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{{Infobox_gene}}
'''Calmodulin 1''' is a [[protein]] that in humans is encoded by the ''CALM1'' [[gene]].<ref name="pmid6385987">{{cite journal | vauthors = Wawrzynczak EJ, Perham RN | title = Isolation and nucleotide sequence of a cDNA encoding human calmodulin | journal = Biochem. Int. | volume = 9 | issue = 2 | pages = 177–85 | date = August 1984 | pmid = 6385987 | doi =  }}</ref>


== Function ==


<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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 [[cell membrane|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 [[cell growth|growth]] and the [[cell cycle]] as well as in [[signal transduction]] and the synthesis and release of [[neurotransmitter]]s.<ref>{{cite web | title = Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=801| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_CALM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a29.
| PDB = {{PDB2|1a29}}, {{PDB2|1ahr}}, {{PDB2|1ak8}}, {{PDB2|1cdl}}, {{PDB2|1cdm}}, {{PDB2|1cfc}}, {{PDB2|1cfd}}, {{PDB2|1cff}}, {{PDB2|1ckk}}, {{PDB2|1cll}}, {{PDB2|1cm1}}, {{PDB2|1cm4}}, {{PDB2|1cmf}}, {{PDB2|1cmg}}, {{PDB2|1ctr}}, {{PDB2|1deg}}, {{PDB2|1dmo}}, {{PDB2|1f70}}, {{PDB2|1f71}}, {{PDB2|1fw4}}, {{PDB2|1g4y}}, {{PDB2|1iq5}}, {{PDB2|1iwq}}, {{PDB2|1j7o}}, {{PDB2|1j7p}}, {{PDB2|1k90}}, {{PDB2|1k93}}, {{PDB2|1l7z}}, {{PDB2|1lin}}, {{PDB2|1lvc}}, {{PDB2|1mux}}, {{PDB2|1mxe}}, {{PDB2|1niw}}, {{PDB2|1nwd}}, {{PDB2|1ooj}}, {{PDB2|1pk0}}, {{PDB2|1prw}}, {{PDB2|1qiv}}, {{PDB2|1qiw}}, {{PDB2|1qs7}}, {{PDB2|1qtx}}, {{PDB2|1qx5}}, {{PDB2|1qx7}}, {{PDB2|1s26}}, {{PDB2|1sk6}}, {{PDB2|1sw8}}, {{PDB2|1sy9}}, {{PDB2|1up5}}, {{PDB2|1vrk}}, {{PDB2|1wrz}}, {{PDB2|1x02}}, {{PDB2|1xa5}}, {{PDB2|1xfu}}, {{PDB2|1xfv}}, {{PDB2|1xfw}}, {{PDB2|1xfx}}, {{PDB2|1xfy}}, {{PDB2|1xfz}}, {{PDB2|1y0v}}, {{PDB2|1y6w}}, {{PDB2|1yr5}}, {{PDB2|1yrt}}, {{PDB2|1yru}}, {{PDB2|1zot}}, {{PDB2|1zuz}}, {{PDB2|2bbm}}, {{PDB2|2bbn}}, {{PDB2|2bcx}}, {{PDB2|2be6}}, {{PDB2|2bkh}}, {{PDB2|2bki}}, {{PDB2|2col}}, {{PDB2|2dfs}}, {{PDB2|2f2o}}, {{PDB2|2f2p}}, {{PDB2|2f3y}}, {{PDB2|2f3z}}, {{PDB2|2fot}}, {{PDB2|2hf5}}, {{PDB2|2ix7}}, {{PDB2|3cln}}, {{PDB2|4cln}}
| Name = Calmodulin 1 (phosphorylase kinase, delta)
| HGNCid = 1442
| Symbol = CALM1
| AltSymbols =; CALML2; CAMI; DD132; PHKD
| OMIM = 114180
| ECnumber = 
| Homologene = 55999
| MGIid = 88251
| Function =
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 801
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_008819
    | Hs_RefseqmRNA = NM_006888
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 12313
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_009790
    | Mm_RefseqProtein = NP_033920
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Calmodulin 1''' (gene name '''CALM1''') is one of nearly twenty human [[calmodulin]]s.


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
Calmodulin 1 has been shown to [[Protein-protein interaction|interact]] with:
{{PBB_Summary
* [[AKAP9]],<ref name = pmid12221128>{{cite journal | vauthors = Takahashi M, Yamagiwa A, Nishimura T, Mukai H, Ono Y | title = Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex | journal = Mol. Biol. Cell | volume = 13 | issue = 9 | pages = 3235–45 | date = Sep 2002 | pmid = 12221128 | pmc = 124155 | doi = 10.1091/mbc.E02-02-0112 }}</ref>  
| section_title =  
* [[Androgen receptor]],<ref name = pmid14695896>{{cite journal | vauthors = Cifuentes E, Mataraza JM, Yoshida BA, Menon M, Sacks DB, Barrack ER, Reddy GP | title = Physical and functional interaction of androgen receptor with calmodulin in prostate cancer cells | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 101 | issue = 2 | pages = 464–9 | date = Jan 2004 | pmid = 14695896 | pmc = 327170 | doi = 10.1073/pnas.0307161101 }}</ref>
| summary_text = Calmodulin is the archetype of the family of calcium-modulated 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 motifs. Its functions include roles in growth and the cell cycle as well as in signal transduction and the synthesis and release of neurotransmitters.[supplied by OMIM]<ref>{{cite web | title = Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=801| accessdate = }}</ref>
* [[IQGAP1]],<ref name = pmid12446675>{{cite journal | vauthors = Li Z, Sacks DB | title = Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1 | journal = J. Biol. Chem. | volume = 278 | issue = 6 | pages = 4347–52 | date = Feb 2003 | pmid = 12446675 | doi = 10.1074/jbc.M208579200 }}</ref><ref name = pmid11734550>{{cite journal | vauthors = Briggs MW, Li Z, Sacks DB | title = IQGAP1-mediated stimulation of transcriptional co-activation by beta-catenin is modulated by calmodulin | journal = J. Biol. Chem. | volume = 277 | issue = 9 | pages = 7453–65 | date = Mar 2002 | pmid = 11734550 | doi = 10.1074/jbc.M104315200 }}</ref>
}}
* [[PPEF1]],<ref name = pmid12051765>{{cite journal | vauthors = Kutuzov MA, Solov'eva OV, Andreeva AV, Bennett N | title = Protein Ser/Thr phosphatases PPEF interact with calmodulin | journal = Biochem. Biophys. Res. Commun. | volume = 293 | issue = 3 | pages = 1047–52 | date = May 2002 | pmid = 12051765 | doi = 10.1016/S0006-291X(02)00338-8 }}</ref> and
* [[TRPV1]].<ref name = pmid12808128>{{cite journal | vauthors = Numazaki M, Tominaga T, Takeuchi K, Murayama N, Toyooka H, Tominaga M | title = Structural determinant of TRPV1 desensitization interacts with calmodulin | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 100 | issue = 13 | pages = 8002–6 | date = Jun 2003 | pmid = 12808128 | pmc = 164702 | doi = 10.1073/pnas.1337252100 }}</ref>


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Zhang M, Yuan T | title = Molecular mechanisms of calmodulin's functional versatility | journal = Biochem. Cell Biol. | volume = 76 | issue = 2–3 | pages = 313–23 | year = 1999 | pmid = 9923700 | doi = 10.1139/bcb-76-2-3-313 }}
| citations =
* {{cite journal | vauthors = Gusev NB | title = Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation | journal = Biochemistry Mosc. | volume = 66 | issue = 10 | pages = 1112–21 | year = 2002 | pmid = 11736632 | doi = 10.1023/A:1012480829618 }}
*{{cite journal | author=Zhang M, Yuan T |title=Molecular mechanisms of calmodulin's functional versatility. |journal=Biochem. Cell Biol. |volume=76 |issue= 2-3 |pages= 313-23 |year= 1999 |pmid= 9923700 |doi= }}
* {{cite journal | vauthors = Benaim G, Villalobo A | title = Phosphorylation of calmodulin. Functional implications | journal = Eur. J. Biochem. | volume = 269 | issue = 15 | pages = 3619–31 | year = 2002 | pmid = 12153558 | doi = 10.1046/j.1432-1033.2002.03038.x }}
*{{cite journal | author=Gusev NB |title=Some properties of caldesmon and calponin and the participation of these proteins in regulation of smooth muscle contraction and cytoskeleton formation. |journal=Biochemistry Mosc. |volume=66 |issue= 10 |pages= 1112-21 |year= 2002 |pmid= 11736632 |doi= }}
* {{cite journal | vauthors = Trudeau MC, Zagotta WN | title = Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels | journal = J. Biol. Chem. | volume = 278 | issue = 21 | pages = 18705–8 | year = 2003 | pmid = 12626507 | doi = 10.1074/jbc.R300001200 }}
*{{cite journal | author=Benaim G, Villalobo A |title=Phosphorylation of calmodulin. Functional implications. |journal=Eur. J. Biochem. |volume=269 |issue= 15 |pages= 3619-31 |year= 2002 |pmid= 12153558 |doi= }}
*{{cite journal | author=Trudeau MC, Zagotta WN |title=Calcium/calmodulin modulation of olfactory and rod cyclic nucleotide-gated ion channels. |journal=J. Biol. Chem. |volume=278 |issue= 21 |pages= 18705-8 |year= 2003 |pmid= 12626507 |doi= 10.1074/jbc.R300001200 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=801}}


==External links==
== External links ==
*[http://www.pir.uniprot.org/cgi-bin/upEntry?id=P62158 UniProt entry]
*[http://www.pir.uniprot.org/cgi-bin/upEntry?id=P62158 UniProt entry]


{{WH}}
 
{{WS}}
{{protein-stub}}
 
[[Category:EF-hand-containing proteins]]

Latest revision as of 10:32, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

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Ensembl

n/a

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UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

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.[2]

Interactions

Calmodulin 1 has been shown to interact with:

References

  1. ↑ Wawrzynczak EJ, Perham RN (August 1984). "Isolation and nucleotide sequence of a cDNA encoding human calmodulin". Biochem. Int. 9 (2): 177–85. PMID 6385987.
  2. ↑ "Entrez Gene: CALM1 calmodulin 1 (phosphorylase kinase, delta)".
  3. ↑ 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.
  4. ↑ 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.
  5. ↑ 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.
  6. ↑ 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.
  7. ↑ 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.
  8. ↑ 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. 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


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