| |
|---|---|
| Accession Number: | P62158 |
| Protein Name: | Calmodulin |
| Length: | 149 |
| Molecular Weight: | 16838.00 |
| Species: | Homo sapiens (Human) [9606] |
| Location1 / Topology2 / Orientation3: | Cytoplasm1 |
| Substrate | |
Cross database links:
| DIP: | DIP-31794N |
|---|---|
| Entrez Gene ID: | 801 805 808 |
| Pfam: | PF00036 |
| KEGG: | hsa:801 hsa:805 hsa:808 |
Gene Ontology
GO:0005813
C:centrosome
GO:0005829
C:cytosol
GO:0005576
C:extracellular region
GO:0005654
C:nucleoplasm
GO:0005886
C:plasma membrane
GO:0005876
C:spindle microtubule
GO:0000922
C:spindle pole
GO:0005509
F:calcium ion binding
GO:0031997
F:N-terminal myristoylation domain binding
GO:0043274
F:phospholipase binding
GO:0019904
F:protein domain specific binding
GO:0031996
F:thioesterase binding
GO:0031432
F:titin binding
GO:0007202
P:activation of phospholipase C activity
GO:0007186
P:G-protein coupled receptor signaling pathway
GO:0006006
P:glucose metabolic process
GO:0005980
P:glycogen catabolic process
GO:0006936
P:muscle contraction
GO:0060315
P:negative regulation of ryanodine-sensitive calcium-release channel activity
GO:0048011
P:nerve growth factor receptor signaling pathway
GO:0046209
P:nitric oxide metabolic process
GO:0030168
P:platelet activation
GO:0002576
P:platelet degranulation
GO:0060316
P:positive regulation of ryanodine-sensitive calcium-release channel activity
GO:0032465
P:regulation of cytokinesis
GO:0050999
P:regulation of nitric-oxide synthase activity
GO:0010880
P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
GO:0051592
P:response to calcium ion
GO:0007268
P:synaptic transmission
| |
References (37)[1] “Isolation and nucleotide sequence of a cDNA encoding human calmodulin.” Wawrzynczak E.J.et.al. 6385987 [2] “Molecular analysis of human and rat calmodulin complementary DNA clones. Evidence for additional active genes in these species.” Sengupta B.et.al. 2445749 [3] “Multiple divergent mRNAs code for a single human calmodulin.” Fischer R.et.al. 3182832 [4] “Structural organization of the human CaMIII calmodulin gene.” Koller M.et.al. 2223880 [5] “Structure of the human CALM1 calmodulin gene and identification of two CALM1-related pseudogenes CALM1P1 and CALM1P2.” Rhyner J.A.et.al. 7925473 [6] “Characterization of the human CALM2 calmodulin gene and comparison of the transcriptional activity of CALM1, CALM2 and CALM3.” Toutenhoofd S.L.et.al. 9681195 [7] “The DNA sequence and analysis of human chromosome 14.” Heilig R.et.al. 12508121 [8] “Generation and annotation of the DNA sequences of human chromosomes 2 and 4.” Hillier L.W.et.al. 15815621 [9] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [10] “Complete amino acid sequence of human brain calmodulin.” Sasagawa T.et.al. 7093203 [11] “Structural basis for activation of the titin kinase domain during myofibrillogenesis.” Mayans O.et.al. 9804419 [12] “Recombinant expression, purification and characterisation of the HMG domain of human SRY.” Kelly S.et.al. 12871148 [13] “Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6.” Shen C.et.al. 16127172 [14] “Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal.” Sim H.et.al. 15746192 [15] “Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.” Rush J.et.al. 15592455 [16] “CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability.” Tsang W.Y.et.al. 16760425 [17] “Cep97 and CP110 suppress a cilia assembly program.” Spektor A.et.al. 17719545 [18] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.” Rikova K.et.al. 18083107 [19] “Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.” Molina H.et.al. 17287340 [20] “Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks.” Wolf-Yadlin A.et.al. 17389395 [21] “A quantitative atlas of mitotic phosphorylation.” Dephoure N.et.al. 18669648 [22] “Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.” Gauci S.et.al. 19413330 [23] “An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells.” Heibeck T.H.et.al. 19534553 [24] “Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.” Mayya V.et.al. 19690332 [25] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.” Choudhary C.et.al. 19608861 [26] “Conserved motif of CDK5RAP2 mediates its localization to centrosomes and the Golgi complex.” Wang Z.et.al. 20466722 [27] “Initial characterization of the human central proteome.” Burkard T.R.et.al. 21269460 [28] “Alpha-helix nucleation by a calcium-binding peptide loop.” Siedlecka M.et.al. 9927666 [29] “Solution structure of Ca(2+)-calmodulin reveals flexible hand-like properties of its domains.” Chou J.J.et.al. 11685248 [30] “Calmodulin structure refined at 1.7 A resolution.” Chattopadhyaya R.et.al. 1474585 [31] “Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.” Cook W.J.et.al. 7803388 [32] “Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin.” Drum C.L.et.al. 11807546 [33] “Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins.” Shen Y.et.al. 12485993 [34] “Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin.” Yamauchi E.et.al. 12577052 [35] “Insights into voltage-gated calcium channel regulation from the structure of the CaV1.2 IQ domain-Ca2+/calmodulin complex.” Van Petegem F.et.al. 16299511 | |
| Structure: | |
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| FASTA formatted sequence |
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1: MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG 61: NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE 121: EVDEMIREAD IDGDGQVNYE EFVQMMTAK