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Identification
HMDB Protein ID HMDBP02775
Secondary Accession Numbers
  • 8281
Name Caldesmon
Synonyms
  1. CDM
Gene Name CALD1
Protein Type Unknown
Biological Properties
General Function Involved in actin binding
Specific Function Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
myosin binding
calmodulin binding
protein binding
cytoskeletal protein binding
actin binding
Process
multicellular organismal process
system process
muscle system process
muscle contraction
Cellular Location
  1. Cytoplasm
  2. Cytoplasm
  3. cytoskeleton
  4. myofibril
Gene Properties
Chromosome Location Chromosome:7
Locus 7q33
SNPs CALD1
Gene Sequence
>2382 bp
ATGGATGATTTTGAGCGTCGCAGAGAACTTAGAAGGCAAAAGAGGGAGGAGATGCGACTC
GAAGCAGAAAGAATCGCCTACCAGAGGAATGACGATGATGAAGAGGAGGCAGCCCGGGAA
CGGCGCCGCCGAGCCCGACAGGAACGGCTGCGGCAGAAGCAGGAGGAAGAATCCTTGGGA
CAGGTGACCGACCAGGTGGAGGTGAATGCCCAGAACAGTGTGCCTGACGAGGAGGCCAAG
ACAACCACCACAAACACTCAAGTGGAAGGGGATGATGAGGCCGCATTCCTGGAGCGCCTG
GCTCGGCGTGAGGAAAGACGCCAAAAACGCCTTCAGGAGGCTCTGGAGCGGCAGAAGGAG
TTCGACCCAACAATAACAGATGCAAGTCTGTCGCTCCCAAGCAGAAGAATGCAAAATGAC
ACAGCAGAAAATGAAACTACCGAGAAGGAAGAAAAAAGTGAAAGTCGCCAAGAAAGATAC
GAGATAGAGGAAACAGAAACAGTCACCAAGTCCTACCAGAAGAATGATTGGAGGGATGCT
GAAGAAAACAAGAAAGAAGACAAGGAAAAGGAGGAGGAGGAAGAGGAGAAGCCAAAGCGA
GGGAGCATTGGAGAAAATCAGGTAGAGGTGATGGTGGAAGAGAAAACAACTGAAAGCCAG
GAGGAAACAGTGGTAATGTCATTAAAAAATGGGCAGATCAGTTCAGAAGAGCCTAAACAA
GAGGAGGAGAGGGAACAAGGTTCAGATGAGATTTCCCATCATGAAAAGATGGAAGAGGAA
GACAAGGAAAGAGCTGAGGCAGAGAGGGCAAGGTTGGAAGCAGAAGAAAGAGAAAGAATT
AAAGCCGAGCAAGACAAAAAGATAGCAGATGAACGAGCAAGAATTGAAGCAGAAGAAAAA
GCAGCTGCCCAAGAAAGAGAAAGGAGAGAGGCAGAAGAGAGGGAAAGGATGAGGGAGGAA
GAGAAAAGGGCAGCAGAGGAGAGGCAGAGGATAAAGGAGGAAGAGAAAAGGGCAGCAGAG
GAGAGGCAGAGGATAAAGGAGGAAGAGAAAAGGGCAGCAGAGGAGAGGCAGAGGATAAAA
GAGGAAGAGAAAAGGGCAGCAGAGGAGAGGCAAAGGGCCAGGGCAGAGGAGGAAGAGAAG
GCTAAGGTAGAAGAGCAGAAACGTAACAAGCAGCTAGAAGAGAAAAAACATGCCATGCAA
GAGACAAAGATAAAAGGGGAAAAGGTAGAACAGAAAATAGAAGGGAAATGGGTAAATGAA
AAGAAAGCACAAGAAGATAAACTTCAGACAGCTGTCCTAAAGAAACAGGGAGAAGAGAAG
GGAACTAAAGTGCAAGCTAAAAGAGAAAAGCTCCAAGAAGACAAGCCTACCTTCAAAAAA
GAAGAGATCAAAGATGAAAAGATTAAAAAGGACAAAGAACCCAAAGAAGAAGTTAAGAGC
TTCATGGATCGAAAGAAGGGATTTACAGAAGTTAAGTCGCAGAATGGAGAATTCATGACC
CACAAACTTAAACATACTGAGAATACTTTCAGCCGCCCTGGAGGGAGGGCCAGCGTGGAC
ACCAAGGAGGCTGAGGGCGCCCCCCAGGTGGAAGCCGGCAAAAGGCTGGAGGAGCTTCGT
CGTCGTCGCGGGGAGACCGAGAGCGAAGAGTTCGAGAAGCTCAAACAGAAGCAGCAGGAG
GCGGCTTTGGAGCTGGAGGAACTCAAGAAAAAGAGGGAGGAGAGAAGGAAGGTCCTGGAG
GAGGAAGAGCAGAGGAGGAAGCAGGAGGAAGCCGATCGAAAACTCAGAGAGGAGGAAGAG
AAGAGGAGGCTAAAGGAAGAGATTGAAAGGCGAAGAGCAGAAGCTGCTGAGAAACGCCAG
AAGATGCCAGAAGATGGCTTGTCAGATGACAAGAAACCATTCAAGTGTTTCACTCCTAAA
GGTTCATCTCTCAAGATAGAAGAGCGAGCAGAATTTTTGAATAAGTCTGTGCAGAAAAGC
AGTGGTGTCAAATCGACCCATCAAGCAGCAATAGTCTCCAAGATTGACAGCAGACTGGAG
CAGTATACCAGTGCAATTGAGGGAACAAAAAGCGCAAAACCTACAAAGCCGGCAGCCTCG
GATCTTCCTGTTCCTGCTGAAGGTGTACGCAACATCAAGAGTATGTGGGAGAAAGGGAAT
GTGTTTTCATCCCCCACTGCAGCAGGCACACCAAATAAGGAAACTGCTGGCTTGAAGGTA
GGGGTTTCTAGCCGCATCAATGAATGGCTAACTAAAACCCCAGATGGAAACAAGTCACCT
GCTCCCAAACCTTCTGACTTGAGACCAGGAGACGTATCCAGCAAGCGGAACCTCTGGGAA
AAGCAATCTGTGGATAAGGTCACTTCCCCCACTAAGGTTTGA
Protein Properties
Number of Residues 793
Molecular Weight 93249.5
Theoretical pI 5.35
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Caldesmon
MDDFERRRELRRQKREEMRLEAERIAYQRNDDDEEEAARERRRRARQERLRQKQEEESLG
QVTDQVEVNAQNSVPDEEAKTTTTNTQVEGDDEAAFLERLARREERRQKRLQEALERQKE
FDPTITDASLSLPSRRMQNDTAENETTEKEEKSESRQERYEIEETETVTKSYQKNDWRDA
EENKKEDKEKEEEEEEKPKRGSIGENQVEVMVEEKTTESQEETVVMSLKNGQISSEEPKQ
EEEREQGSDEISHHEKMEEEDKERAEAERARLEAEERERIKAEQDKKIADERARIEAEEK
AAAQERERREAEERERMREEEKRAAEERQRIKEEEKRAAEERQRIKEEEKRAAEERQRIK
EEEKRAAEERQRARAEEEEKAKVEEQKRNKQLEEKKRAMQETKIKGEKVEQKIEGKWVNE
KKAQEDKLQTAVLKKQGEEKGTKVQAKREKLQEDKPTFKKEEIKDEKIKKDKEPKEEVKS
FMDRKKGFTEVKSQNGEFMTHKLKHTENTFSRPGGRASVDTKEAEGAPQVEAGKRLEELR
RRRGETESEEFEKLKQKQQEAALELEELKKKREERRKVLEEEEQRRKQEEADRKLREEEE
KRRLKEEIERRRAEAAEKRQKMPEDGLSDDKKPFKCFTPKGSSLKIEERAEFLNKSVQKS
SGVKSTHQAAIVSKIDSRLEQYTSAIEGTKSAKPTKPAASDLPVPAEGVRNIKSMWEKGN
VFSSPTAAGTPNKETAGLKVGVSSRINEWLTKTPDGNKSPAPKPSDLRPGDVSSKRNLWE
KQSVDKVTSPTKV
GenBank ID Protein 44680105
UniProtKB/Swiss-Prot ID Q05682
UniProtKB/Swiss-Prot Entry Name CALD1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_033138.3
GeneCard ID CALD1
GenAtlas ID CALD1
HGNC ID HGNC:1441
References
General References
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  2. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  3. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  4. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  5. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  6. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  7. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
  8. Novy RE, Lin JL, Lin JJ: Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells. J Biol Chem. 1991 Sep 5;266(25):16917-24. [PubMed:1885618 ]
  9. Humphrey MB, Herrera-Sosa H, Gonzalez G, Lee R, Bryan J: Cloning of cDNAs encoding human caldesmons. Gene. 1992 Mar 15;112(2):197-204. [PubMed:1555769 ]
  10. Hayashi K, Yano H, Hashida T, Takeuchi R, Takeda O, Asada K, Takahashi E, Kato I, Sobue K: Genomic structure of the human caldesmon gene. Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):12122-6. [PubMed:1465449 ]
  11. Huber PA, Redwood CS, Avent ND, Tanner MJ, Marston SB: Identification of functioning regulatory sites and a new myosin binding site in the C-terminal 288 amino acids of caldesmon expressed from a human clone. J Muscle Res Cell Motil. 1993 Aug;14(4):385-91. [PubMed:8227296 ]