CALM2

Available structures

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

CALM2, CAMII, PHKD, PHKD2, LQT15, caM, calmodulin 2 (phosphorylase kinase, delta)

External IDs

HomoloGene: 134804 GeneCards: CALM2

Gene ontology
Molecular function	• calcium ion binding • protein phosphatase activator activity • N-terminal myristoylation domain binding • phospholipase binding • ion channel binding • protein domain specific binding • protein N-terminus binding • calcium-dependent protein binding • nitric-oxide synthase regulator activity • nitric-oxide synthase binding • adenylate cyclase binding • enzyme regulator activity • titin binding • metal ion binding • type 3 metabotropic glutamate receptor binding • protein serine/threonine kinase activator activity • protein binding • thioesterase binding • protein kinase binding • phosphatidylinositol 3-kinase binding • ligand-gated ion channel activity • Ras guanyl-nucleotide exchange factor activity • inositol-1,4,5-trisphosphate 3-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
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 cyclic nucleotide metabolic process • 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
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


805


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Ensembl


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UniProt


P62158


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RefSeq (mRNA)


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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


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Location (UCSC)

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PubMed search

^[1]

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Wikidata

View/Edit Human

Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene.^[2]^[3]

Clinical significance

Mutations in CALM2 are associated to cardiac arrhythmias .^[4]

Interactions

CALM2 has been shown to interact with AKAP9.^[5]^[6]

References

↑ "Human PubMed Reference:".
↑ "Entrez Gene: CALM2 Calmodulin 2 (phosphorylase kinase, delta)".
↑ SenGupta B, Friedberg F, Detera-Wadleigh SD (December 1987). "Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species". J. Biol. Chem. 262 (34): 16663–70. PMID 2445749.
↑ Makita N, Yagihara N, Crotti L, Johnson CN, Beckmann BM, Roh MS, Shigemizu D, Lichtner P, Ishikawa T, Aiba T, Homfray T, Behr ER, Klug D, Denjoy I, Mastantuono E, Theisen D, Tsunoda T, Satake W, Toda T, Nakagawa H, Tsuji Y, Tsuchiya T, Yamamoto H, Miyamoto Y, Endo N, Kimura A, Ozaki K, Motomura H, Suda K, Tanaka T, Schwartz PJ, Meitinger T, Kääb S, Guicheney P, Shimizu W, Bhuiyan ZA, Watanabe H, Chazin WJ, George AL (2014). "Novel calmodulin mutations associated with congenital arrhythmia susceptibility". Circ Cardiovasc Genet. 7 (4): 466–74. PMC 4140998 . PMID 24917665. doi:10.1161/CIRCGENETICS.113.000459.
↑ 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. PMC 124155 . PMID 12221128. doi:10.1091/mbc.E02-02-0112.
↑ Berchtold MW, Egli R, Rhyner JA, Hameister H, Strehler EE (May 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. PMID 8314583. doi:10.1006/geno.1993.1211.

External links

Human CALM2 genome location and CALM2 gene details page in the UCSC Genome Browser.

Zhang M, Yuan T (1998). "Molecular mechanisms of calmodulin's functional versatility". Biochem. Cell Biol. 76 (2-3): 313–23. PMID 9923700. doi:10.1139/bcb-76-2-3-313.
Gusev NB (2001). "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. PMID 11736632. doi:10.1023/A:1012480829618.
Benaim G, Villalobo A (2002). "Phosphorylation of calmodulin. Functional implications". Eur. J. Biochem. 269 (15): 3619–31. PMID 12153558. doi:10.1046/j.1432-1033.2002.03038.x.
Koller M, Schnyder B, Strehler EE (1990). "Structural organization of the human CaMIII calmodulin gene". Biochim. Biophys. Acta. 1087 (2): 180–9. PMID 2223880. doi:10.1016/0167-4781(90)90203-e.
Baudier J, Mochly-Rosen D, Newton A, Lee SH, Koshland DE, Cole RD (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. PMID 3111527. doi:10.1021/bi00384a033.
Matoba R, Okubo K, Hori N, Fukushima A, Matsubara K (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene. 146 (2): 199–207. PMID 8076819. doi:10.1016/0378-1119(94)90293-3.
Srinivas SK, Srinivas RV, Anantharamaiah GM, Compans RW, Segrest JP (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, Robey WG, Montelaro RC (1993). "Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein". AIDS Res. Hum. Retroviruses. 9 (11): 1057–66. PMID 8312049. doi:10.1089/aid.1993.9.1057.
Radding W, Pan ZQ, Hunter E, Johnston P, Williams JP, McDonald JM (1996). "Expression of HIV-1 envelope glycoprotein alters cellular calmodulin". Biochem. Biophys. Res. Commun. 218 (1): 192–7. PMID 8573130. doi:10.1006/bbrc.1996.0034.
Pan Z, Radding W, Zhou T, Hunter E, Mountz J, McDonald JM (1996). "Role of calmodulin in HIV-potentiated Fas-mediated apoptosis". Am. J. Pathol. 149 (3): 903–10. PMC 1865159 . PMID 8780394.
Sasaki M, Uchiyama J, Ishikawa H, Matsushita S, Kimura G, Nomoto K, Koga Y (1996). "Induction of apoptosis by calmodulin-dependent intracellular Ca2+ elevation in CD4+ cells expressing gp 160 of HIV". Virology. 224 (1): 18–24. PMID 8862395. doi:10.1006/viro.1996.0502.
Brigino E, Haraguchi S, Koutsonikolis A, Cianciolo GJ, Owens U, Good RA, Day NK (1997). "Interleukin 10 is induced by recombinant HIV-1 Nef protein involving the calcium/calmodulin-dependent phosphodiesterase signal transduction pathway". Proc. Natl. Acad. Sci. U.S.A. 94 (7): 3178–82. PMC 20342 . PMID 9096366. doi:10.1073/pnas.94.7.3178.
Minakami R, Jinnai N, Sugiyama H (1997). "Phosphorylation and calmodulin binding of the metabotropic glutamate receptor subtype 5 (mGluR5) are antagonistic in vitro". J. Biol. Chem. 272 (32): 20291–8. PMID 9242710. doi:10.1074/jbc.272.32.20291.
Miyawaki A, Llopis J, Heim R, McCaffery JM, Adams JA, Ikura M, Tsien RY (1997). "Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin". Nature. 388 (6645): 882–7. PMID 9278050. doi:10.1038/42264.
Malvoisin E, Wild F (1997). "Inhibition of HIV-1, HIV-2 and SIV envelope glycoprotein-mediated cell fusion by calmodulin". Virus Res. 50 (2): 119–27. PMID 9282777. doi:10.1016/S0168-1702(97)00060-9.
Martoglio B, Graf R, Dobberstein B (1997). "Signal peptide fragments of preprolactin and HIV-1 p-gp160 interact with calmodulin". EMBO J. 16 (22): 6636–45. PMC 1170268 . PMID 9362478. doi:10.1093/emboj/16.22.6636.
Ishikawa H, Sasaki M, Noda S, Koga Y (1998). "Apoptosis induction by the binding of the carboxyl terminus of human immunodeficiency virus type 1 gp160 to calmodulin". J. Virol. 72 (8): 6574–80. PMC 109834 . PMID 9658102.
Toutenhoofd SL, Foletti D, Wicki R, Rhyner JA, Garcia F, Tolon R, Strehler EE (1998). "Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3". Cell Calcium. 23 (5): 323–38. PMID 9681195. doi:10.1016/S0143-4160(98)90028-8.

PDB gallery

1a29: CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:2 COMPLEX)

1ahr: CALMODULIN MUTANT WITH A TWO RESIDUE DELETION IN THE CENTRAL HELIX

1ak8: NMR SOLUTION STRUCTURE OF CERIUM-LOADED CALMODULIN AMINO-TERMINAL DOMAIN (CE2-TR1C), 23 STRUCTURES

1cdl: TARGET ENZYME RECOGNITION BY CALMODULIN: 2.4 ANGSTROMS STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX

1cdm: MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES

1cfc: CALCIUM-FREE CALMODULIN

1cfd: CALCIUM-FREE CALMODULIN

1cff: NMR SOLUTION STRUCTURE OF A COMPLEX OF CALMODULIN WITH A BINDING PEPTIDE OF THE CA2+-PUMP

1ckk: CALMODULIN/RAT CA2+/CALMODULIN DEPENDENT PROTEIN KINASE FRAGMENT

1cll: CALMODULIN STRUCTURE REFINED AT 1.7 ANGSTROMS RESOLUTION

1cm1: MOTIONS OF CALMODULIN-SINGLE-CONFORMER REFINEMENT

1cm4: MOTIONS OF CALMODULIN-FOUR-CONFORMER REFINEMENT

1cmf: NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN

1cmg: NMR SOLUTION STRUCTURE OF CALCIUM-LOADED CALMODULIN CARBOXY-TERMINAL DOMAIN

1ctr: DRUG BINDING BY CALMODULIN: CRYSTAL STRUCTURE OF A CALMODULIN-TRIFLUOPERAZINE COMPLEX

1deg: THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE

1dmo: CALMODULIN, NMR, 30 STRUCTURES

1f70: REFINED SOLUTION STRUCTURE OF CALMODULIN N-TERMINAL DOMAIN

1f71: REFINED SOLUTION STRUCTURE OF CALMODULIN C-TERMINAL DOMAIN

1fw4: CRYSTAL STRUCTURE OF E. COLI FRAGMENT TR2C FROM CALMODULIN TO 1.7 A RESOLUTION

1g4y: 1.60 A CRYSTAL STRUCTURE OF THE GATING DOMAIN FROM SMALL CONDUCTANCE POTASSIUM CHANNEL COMPLEXED WITH CALCIUM-CALMODULIN

1iq5: Calmodulin/nematode CA2+/Calmodulin dependent kinase kinase fragment

1iwq: Crystal Structure of MARCKS calmodulin binding domain peptide complexed with Ca2+/Calmodulin

1j7o: Solution structure of Calcium-calmodulin N-terminal domain

1j7p: Solution structure of Calcium calmodulin C-terminal domain

1k90: Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 3' deoxy-ATP

1k93: Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin

1l7z: Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide

1lin: CALMODULIN COMPLEXED WITH TRIFLUOPERAZINE (1:4 COMPLEX)

1lvc: Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin and 2' deoxy, 3' anthraniloyl ATP

1mux: SOLUTION NMR STRUCTURE OF CALMODULIN/W-7 COMPLEX: THE BASIS OF DIVERSITY IN MOLECULAR RECOGNITION, 30 STRUCTURES

1mxe: Structure of the Complex of Calmodulin with the Target Sequence of CaMKI

1niw: Crystal structure of endothelial nitric oxide synthase peptide bound to calmodulin

1nwd: Solution Structure of Ca2+/Calmodulin bound to the C-terminal Domain of Petunia Glutamate Decarboxylase

1ooj: Structural genomics of Caenorhabditis elegans : Calmodulin

1pk0: Crystal Structure of the EF3-CaM complexed with PMEApp

1prw: Crystal structure of bovine brain Ca++ calmodulin in a compact form

1qiv: CALMODULIN COMPLEXED WITH N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(3,4-BIS-BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE (DPD), 1:2 COMPLEX

1qiw: CALMODULIN COMPLEXED WITH N-(3,3,-DIPHENYLPROPYL)-N'-[1-R-(3,4-BIS-BUTOXYPHENYL)-ETHYL]-PROPYLENEDIAMINE (DPD)

1qs7: The 1.8 angstrom structure of calmodulin rs20 peptide complex

1qtx: THE 1.65 ANGSTROM STRUCTURE OF CALMODULIN RS20 PEPTIDE COMPLEX

1qx5: Crystal structure of apoCalmodulin

1qx7: Crystal structure of apoCaM bound to the gating domain of small conductance Ca2+-activated potassium channel

1s26: Structure of Anthrax Edema Factor-Calmodulin-alpha,beta-methyleneadenosine 5'-triphosphate Complex Reveals an Alternative Mode of ATP Binding to the Catalytic Site

1sk6: Crystal structure of the adenylyl cyclase domain of anthrax edema factor (EF) in complex with calmodulin, 3',5' cyclic AMP (cAMP), and pyrophosphate

1sw8: Solution structure of the N-terminal domain of Human N60D calmodulin refined with paramagnetism based strategy

1sy9: Structure of calmodulin complexed with a fragment of the olfactory CNG channel

1up5: CHICKEN CALMODULIN

1vrk: THE 1.9 ANGSTROM STRUCTURE OF E84K-CALMODULIN RS20 PEPTIDE COMPLEX

1wrz: Calmodulin complexed with a peptide from a human death-associated protein kinase

1x02: Solution structure of stereo array isotope labeled (SAIL) calmodulin

1xa5: Structure of Calmodulin in complex with KAR-2, a bis-indol alkaloid

1xfu: Crystal structure of anthrax edema factor (EF) truncation mutant, EF-delta 64 in complex with calmodulin

1xfv: Crystal structure of anthrax edema factor (EF) in complex with calmodulin and 3' deoxy-ATP

1xfw: Crystal structure of anthrax edema factor (EF) in complex with calmodulin and 3'5' cyclic AMP (cAMP)

1xfx: Crystal structure of anthrax edema factor (EF) in complex with calmodulin in the presence of 10 millimolar exogenously added calcium chloride

1xfy: Crystal structure of anthrax edema factor (EF) in complex with calmodulin

1xfz: Crystal structure of anthrax edema factor (EF) in complex with calmodulin in the presence of 1 millimolar exogenously added calcium chloride

1y0v: Crystal structure of anthrax edema factor (EF) in complex with calmodulin and pyrophosphate

1y6w: Trapped intermediate of calmodulin

1yr5: 1.7-A structure of calmodulin bound to a peptide from DAP kinase

1yrt: Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin

1yru: Crystal Structure analysis of the adenylyl cyclaes catalytic domain of adenylyl cyclase toxin of Bordetella pertussis in presence of c-terminal calmodulin and 1mM calcium chloride

1zot: crystal structure analysis of the CyaA/C-Cam with PMEAPP

1zuz: Calmodulin in complex with a mutant peptide from human DRP-1 kinase

2bbm: SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULTIDIMENSIONAL NMR

2bbn: SOLUTION STRUCTURE OF A CALMODULIN-TARGET PEPTIDE COMPLEX BY MULTIDIMENSIONAL NMR

2bcx: Crystal structure of calmodulin in complex with a ryanodine receptor peptide

2be6: 2.0 A crystal structure of the CaV1.2 IQ domain-Ca/CaM complex

2bkh: MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2) CRYSTAL STRUCTURE

2bki: MYOSIN VI NUCLEOTIDE-FREE (MDINSERT2-IQ) CRYSTAL STRUCTURE

2col: Crystal structure analysis of CyaA/C-Cam with Pyrophosphate

2dfs: 3-D structure of Myosin-V inhibited state

2f2o: Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

2f2p: Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

2f3y: Calmodulin/IQ domain complex

2f3z: Calmodulin/IQ-AA domain complex

2fot: Crystal structure of the complex between calmodulin and alphaII-spectrin

2hf5: The structure and function of a novel two-site calcium-binding fragment of calmodulin

2ix7: STRUCTURE OF APO-CALMODULIN BOUND TO UNCONVENTIONAL MYOSIN V

3cln: STRUCTURE OF CALMODULIN REFINED AT 2.2 ANGSTROMS RESOLUTION

4cln: STRUCTURE OF A RECOMBINANT CALMODULIN FROM DROSOPHILA MELANOGASTER REFINED AT 2.2-ANGSTROMS RESOLUTION

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CALM2

Clinical significance

Interactions

See also

References

External links

Further reading