Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Calsequestrin-1  

UniProtKB / Swiss-Prot ID :  CASQ1_RABIT

Gene Name (Synonyms) : 
CASQ1  

Species :  Oryctolagus cuniculus (Rabbit). 

Subcellular Localization :  Sarcoplasmic reticulum lumen. Note=This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of fast skeletal muscle cells. 

Protein Function :  Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle isoform (CASQ1) binds around 80 Ca(2+) ions, while the cardiac isoform (CASQ2) binds approximately 60 Ca(2+) ions (By similarity). 

Protein Sequence MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPE...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCEEEECHHHHHHHHHHCCCEEEEEECCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
217PhosphothreonineAKKLTLKLN
HCCCCCCCC
30.63Phosphositeplus
Link
257PhosphothreonineHRRSTLRKL
CCCCEEEEE
28.86Phosphositeplus
Link
344N-linked (GlcNAc...).IGVVNVTDA
CCEEEEECC
28.68UniProtKB
Link
381PhosphothreonineGEINTEDDD
CEEEEEECC
46.59Phosphositeplus
Link-
381Phosphothreonine (CK2_group)GEINTEDDD
CEEEEEECC
46.59PhosphoELM
Link-
381Phosphothreonine; by CK2.GEINTEDDD
CEEEEEECC
46.59UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Amino acid sequence of rabbit fast-twitch skeletal musclecalsequestrin deduced from cDNA and peptide sequencing.";
Fliegel L., Ohnishi M., Carpenter M.R., Khanna V.K.,Reithmeier R.A.F., McLennan D.H.;
Proc. Natl. Acad. Sci. U.S.A. 84:1167-1171(1987).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures