targeting STIM1 to ER-plasma-membrane contacts upon Ca(2+)-store depletion
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EXPRESSION
Type
widely
expressed in
(based on citations)
organ(s)
System
Organ level 1
Organ level 2
Organ level 3
Organ level 4
Level
Pubmed
Species
Stage
Rna symbol
Cardiovascular
heart
Digestive
liver
Nervous
brain
Respiratory
lung
Urinary
kidney
tissue
System
Tissue
Tissue level 1
Tissue level 2
Level
Pubmed
Species
Stage
Rna symbol
Muscular
striatum
cardiac
Muscular
striatum
skeletal
cell lineage
cell lines
fluid/secretion
at STAGE
physiological period
pregnancy
Text
placenta
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
extended N-terminus with potential transmembrane (TM ) type II signal anchor domain directing the catalytic domain into the endoplasmic reticulum, N terminus comprising &
8764;26 amino acids (a truncation of these AAs prevents junctional accumulation of ASPH)
a Ca(2+)-binding EF-hand motif
a compact C terminus catalytic domain, and Ca2+-sensing role of junctate was demonstrated after uncovering an EF-hand domain in the ER-luminal region, in its C terminus
potentially cleaved into a 56kDa protein in the lumen of ER
with SERCA2 co-localized in the sarcoplasmic reticulum of cardiomyocytes
intra-sarcoplasmic reticulum (SR) protein
inserted into the membrane of the sarcoplasmic reticulum (SR) Ca(2+) store where it modifies Ca(2+) signalling in the heart and skeletal muscle
basic FUNCTION
potentially involved in divalent cation binding and protein-protein interaction for a number of vitamin K dependent proteins, like proC, F7, F9, F10, complement factors C1R, C1S
may play an important role in the regulation of SR Ca(2+) cycling through the interaction with ATP2A2 in the murine heart
SR membrane protein, which is part of the SR Ca(2+) release quaternary structure that also includes the ryanodine receptor, triadin and calsequestrin
serves as a bridge between calsequestrin and the Ca(2+) release channel, ryanodine receptor
involved in calcium homeostasis with calsquestrin, triadin, ryanodine receptor
involved in calcium homeostasis in eukaryotic cells
essential factor in maintaining normal cardiac Ca handling and cardiac function
triadin and junctin are integral sarcoplasmic reticulum membrane proteins that form a macromolecular complex with the skeletal muscle ryanodine receptor (RYR1)
has a role in maintaining sarcoplasmic reticulum Ca2+ store size in myotubes
ASPH and TRDN each activate skeletal ryanodine receptors but ASPH alone mediates functional interactions with CASQ1
normally acts as an activator of RYR channels at low luminal [Ca(2+)], and as an inhibitor at high luminal [Ca(2+)]
Ca2+-sensing ER protein, and structural component of the ER-PM junctions where ORAI1 and STIM1 cluster and interact in T cells
cell surface protein that catalyzes the hydroxylation of epidermal growth factor (EGF)-like repeats in Notch receptors and ligands
mediates an alternative mechanism for generating localized Ca(2+) elevations within cells, promoting Ca(2+) release from internal stores recruited to phagosomes, thereby boosting phagocytosis
CELLULAR PROCESS
protein, post translation
PHYSIOLOGICAL PROCESS
text
hydroxylation of ASP or ASN in EGF-like domains of several proteins
PATHWAY
metabolism
aminoacid
signaling
a component
CASQ2, TRDN and ASPH form a protein complex that is associated with cardiac ryanodine receptor 2 (RYR2) SR Ca(2+) release channels
forms a quaternary protein complex with the ryanodine receptor, calsequestrin, and triadin in the SR lumen of cardiac muscle
indirect role for triadin in regulating myoplasmic Ca(2+) homeostasis and organizing the molecular complex of the triad but not in regulating skeletal-type excitation-contraction coupling
Ca(2+)-sensing ER protein, and is a structural component of the ER-plasma membrane junctions where ORAI1 and STIM1 cluster and interact in T cells
plays an additional role in STIM1 recruitment by defining the ER-PM junctions for clustering of ORAI1 and STIM1 in a Ca2+-dependent manner
mediates an alternative mechanism for generating localized Ca(2+) elevations within cells, promoting Ca(2+) release from internal stores recruited to phagosomes, thereby boosting phagocytosis
INTERACTION
DNA
RNA
small molecule
metal binding,
iron Fe2+
protein
interacting with ATP2A2 (binding of the C-terminal region of junctate (AAs 79-270) and luminal domain of ATP2A2 (AAs 70-89)
constant interactions between CASQ2 and ASPH, regardless of the SR Ca(2+) concentration, implying that ASPH is an essential component of the CASQ2 scaffold
ASPH is an interacting partner of ORAI1-STIM1 complex
TRDN and ASPH are structurally related transmembrane proteins thought to be key mediators of structural and functional interactions between calsequestrin (CASQ1) and ryanodine receptor (RyRs) at the junctional sarcoplasmic reticulum
C-terminal domain of ASPH binds to residues including the S1-S2 linker of RYR1 and N-terminal domain of ASPH binds between RYR1 residues 1078 and 2156
