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P21817 (RYR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ryanodine receptor 1

Short name=RYR-1
Short name=RyR1
Alternative name(s):
Skeletal muscle calcium release channel
Skeletal muscle ryanodine receptor
Skeletal muscle-type ryanodine receptor
Type 1 ryanodine receptor
Gene names
Name:RYR1
Synonyms:RYDR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length5038 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm. Can also mediate the release of Ca2+ from intracellular stores in neurons, and may thereby promote prolonged Ca2+ signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis By similarity. Ref.13

Subunit structure

Homotetramer. Can also form heterotetramers with RYR2. Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity. Interacts with S100A1. Interacts with FKBP1A; this stabilizes the closed conformation of the channel. Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel. Interacts with CACNB1. Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity By similarity. Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Repeated very high-level exercise decreases interaction with PDE4D and protein phosphatase 1 (PP1). Ref.12 Ref.13

Subcellular location

Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein Probable. Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic.

Tissue specificity

Skeletal muscle and brain (cerebellum and hippocampus). Ref.10

Domain

The calcium release channel activity resides in the C-terminal region while the remaining part of the protein constitutes the 'foot' structure spanning the junctional gap between the sarcoplasmic reticulum (SR) and the T-tubule By similarity.

Post-translational modification

Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2843 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2843.

Activated by reversible S-nitrosylation. Repeated very high-level exercise increases S-nitrosylation.

Involvement in disease

Malignant hyperthermia 1 (MHS1) [MIM:145600]: Autosomal dominant pharmacogenetic disorder of skeletal muscle and is one of the main causes of death due to anesthesia. In susceptible people, an MH episode can be triggered by all commonly used inhalational anesthetics such as halothane and by depolarizing muscle relaxants such as succinylcholine. The clinical features of the myopathy are hyperthermia, accelerated muscle metabolism, contractures, metabolic acidosis, tachycardia and death, if not treated with the postsynaptic muscle relaxant, dantrolene. Susceptibility to MH can be determined with the 'in vitro' contracture test (IVCT): observing the magnitude of contractures induced in strips of muscle tissue by caffeine alone and halothane alone. Patients with normal response are MH normal (MHN), those with abnormal response to caffeine alone or halothane alone are MH equivocal (MHE(C) and MHE(H) respectively).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.7 Ref.8 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.38 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.48 Ref.51 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.65 Ref.66

Central core disease of muscle (CCD) [MIM:117000]: Autosomal dominant congenital myopathy, but a severe autosomal recessive form also exists. Both clinical and histological variability is observed. Affected individuals typically display hypotonia and proximal muscle weakness in infancy, leading to the delay of motor milestones. The clinical course of the disorder is usually slow or nonprogressive in adulthood, and the severity of the symptoms may vary from normal to significant muscle weakness. Microscopic examination of CCD-affected skeletal muscle reveals a predominance of type I fibers containing amorphous-looking areas (cores) that do not stain with oxidative and phosphorylase histochemical techniques.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.17 Ref.18 Ref.25 Ref.28 Ref.29 Ref.33 Ref.36 Ref.37 Ref.42 Ref.47 Ref.49 Ref.50 Ref.52 Ref.54 Ref.57 Ref.61 Ref.62 Ref.63 Ref.64 Ref.66 Ref.68

Multiminicore disease with external ophthalmoplegia (MMDO) [MIM:255320]: Clinically heterogeneous neuromuscular disorder. General features include neonatal hypotonia, delayed motor development, and generalized muscle weakness and amyotrophy, which may progress slowly or remain stable. Muscle biopsy shows multiple, poorly circumscribed, short areas of sarcomere disorganization and mitochondria depletion (areas termed minicores) in most muscle fibers. Typically, no dystrophic signs, such as muscle fiber necrosis or regeneration or significant endomysial fibrosis, are present in multiminicore disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.53 Ref.54 Ref.60

Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.54 Ref.67

Defects in RYR1 may be a cause of Samaritan myopathy, a congenital myopathy with benign course. Patients display severe hypotonia and respiratory distress at birth. Unlike other congenital myopathies, the health status constantly improves and patients are minimally affected at adulthood. Ref.54

Miscellaneous

Channel activity is modulated by the alkaloid ryanodine that binds to the open Ca-release channel with high affinity. At low concentrations, ryanodine maintains the channel in an open conformation. High ryanodine concentrations inhibit channel activity. Channel activity is regulated by calmodulin (CALM). The calcium release is activated by increased cytoplasmic calcium levels, by nitric oxyde (NO), caffeine and ATP. Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites By similarity.

Coexpression of normal and mutant Thr-4898 RYR1 in a 1:1 ratio, produces RYR1 channels with normal halothane and caffeine sensitivities, but maximal levels of Ca2+ release are reduced by 67%. Binding of [3H]ryanodine indicates that the heterozygous channel is activated by Ca2+ concentrations 4-fold lower than normal. Single-cell analysis of cotransfected cells shows a significantly increased resting cytoplasmic Ca2+ level and a significantly reduced luminal Ca2+ level. These data indicated a leaky channel, possibly caused by a reduction in the Ca2+ concentration required for channel activation. Comparison with 2 other coexpressed mutant/normal channels suggests that the Thr-4898 mutation produces one of the most abnormal RYR1 channels that has been investigated, and this level of abnormality is reflected in the severe and penetrant phenotype of affected CCD individuals.

Sequence similarities

Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR1 subfamily. [View classification]

Contains 3 B30.2/SPRY domains.

Contains 5 MIR domains.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Calmodulin-binding
   Molecular functionCalcium channel
Developmental protein
Ion channel
Ligand-gated ion channel
Receptor
   PTMPhosphoprotein
S-nitrosylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to caffeine

Inferred from sequence or structural similarity. Source: UniProtKB

cytosolic calcium ion homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

ion transmembrane transport

Traceable author statement. Source: Reactome

muscle contraction

Inferred from sequence or structural similarity. Source: UniProtKB

ossification involved in bone maturation

Inferred from sequence or structural similarity. Source: UniProtKB

outflow tract morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

response to caffeine

Inferred from sequence or structural similarity. Source: BHF-UCL

response to hypoxia

Inferred from direct assay PubMed 19120137. Source: BHF-UCL

skeletal muscle fiber development

Inferred from sequence or structural similarity. Source: UniProtKB

skin development

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentI band

Inferred from direct assay PubMed 11206130. Source: UniProtKB

T-tubule

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from direct assay PubMed 11206130. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11206130. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

junctional membrane complex

Inferred from electronic annotation. Source: Ensembl

junctional sarcoplasmic reticulum membrane

Traceable author statement PubMed 19095005. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 11206130. Source: UniProtKB

sarcoplasmic reticulum

Inferred from sequence or structural similarity. Source: BHF-UCL

sarcoplasmic reticulum membrane

Inferred from sequence or structural similarity. Source: UniProtKB

smooth endoplasmic reticulum

Traceable author statement Ref.1. Source: ProtInc

terminal cisterna

Inferred from sequence or structural similarity PubMed 1374404. Source: BHF-UCL

   Molecular_functioncalcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-release channel activity

Traceable author statement PubMed 9030597. Source: ProtInc

calmodulin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 23414517. Source: IntAct

ryanodine-sensitive calcium-release channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

voltage-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MYOM2P542962EBI-1221290,EBI-5357134

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: P21817-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P21817-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3481-3485: Missing.
Isoform 3 (identifier: P21817-3)

The sequence of this isoform differs from the canonical sequence as follows:
     3865-3869: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 50385038Ryanodine receptor 1
PRO_0000219358

Regions

Topological domain1 – 43264326Cytoplasmic Potential
Transmembrane4327 – 434721Helical; Potential
Transmembrane4348 – 436821Helical; Potential
Transmembrane4560 – 458021Helical; Potential
Transmembrane4652 – 467221Helical; Potential
Transmembrane4781 – 480121Helical; Potential
Transmembrane4808 – 482821Helical; Potential
Transmembrane4840 – 486021Helical; Potential
Intramembrane4891 – 490010Pore-forming; By similarity
Transmembrane4921 – 494121Helical; Potential
Topological domain4942 – 503897Cytoplasmic Potential
Domain97 – 15256MIR 1
Domain159 – 20446MIR 2
Domain210 – 26455MIR 3
Domain270 – 32758MIR 4
Domain335 – 39258MIR 5
Domain581 – 797217B30.2/SPRY 1
Repeat841 – 9541141
Repeat955 – 10681142
Domain1013 – 1208196B30.2/SPRY 2
Repeat1344 – 1359163; truncated
Domain1356 – 1570215B30.2/SPRY 3
Repeat1372 – 1387164; truncated
Repeat2726 – 28451205
Repeat2846 – 29591146
Region841 – 295921196 X approximate repeats
Region3614 – 364330Interaction with CALM
Compositional bias1873 – 192452Glu-rich (acidic)
Compositional bias4462 – 453271Pro-rich

Amino acid modifications

Modified residue28431Phosphoserine; by PKA and PKG By similarity
Modified residue36351S-nitrosocysteine Ref.11
Modified residue48641Phosphotyrosine Ref.14
Modified residue48671Phosphoserine Ref.14

Natural variations

Alternative sequence3481 – 34855Missing in isoform 2.
VSP_005951
Alternative sequence3865 – 38695Missing in isoform 3.
VSP_005952
Natural variant131L → R in MHS1. Ref.65
VAR_058560
Natural variant131L → V in CCD; autosomal recessive form. Ref.64
VAR_045694
Natural variant351C → R in MHS1. Ref.22 Ref.59
VAR_005589
Natural variant441R → C in CCD and MHS1. Ref.51
VAR_045695
Natural variant1091R → W in MMDO. Ref.60
VAR_032910
Natural variant1601E → G in CCD. Ref.57 Ref.68
VAR_045696
Natural variant1631R → C in CCD and MHS1; 2-3% of the cases. Ref.17 Ref.35 Ref.40 Ref.41 Ref.44 Ref.55 Ref.59
VAR_005590
Natural variant1631R → L in MHS1; induces an increase sensitivity to caffeine. Ref.59
VAR_045697
Natural variant1651G → R in MHS1. Ref.59
VAR_045698
Natural variant1661D → N in MHS1. Ref.40 Ref.59
VAR_045699
Natural variant1771R → C in MHS1. Ref.59
VAR_045700
Natural variant1781Y → C in MHS1. Ref.59
VAR_045701
Natural variant2151G → E in CCD; autosomal recessive form. Ref.50
VAR_045702
Natural variant2261M → K in MHS1. Ref.65
VAR_058561
Natural variant2271D → V in MHS1. Ref.59
VAR_045703
Natural variant2481G → R in MHS1; unknown pathological significance. Ref.2 Ref.35 Ref.55 Ref.59
Corresponds to variant rs1801086 [ dbSNP | Ensembl ].
VAR_005591
Natural variant2911A → T.
Corresponds to variant rs2229140 [ dbSNP | Ensembl ].
VAR_051890
Natural variant3281R → W in MHS1; has increased sensitivity to both caffeine and halothane. Ref.48 Ref.59
VAR_045704
Natural variant3411G → R in MHS1; 10% of the cases. Ref.19 Ref.40 Ref.41 Ref.59
Corresponds to variant rs28933997 [ dbSNP | Ensembl ].
VAR_005592
Natural variant3671R → L in MHS1. Ref.65
VAR_058562
Natural variant3821H → N in MHS1. Ref.66
VAR_068510
Natural variant4011R → C in MHS1. Ref.43 Ref.44
VAR_045705
Natural variant4011R → H in MHS1. Ref.40 Ref.59
VAR_045706
Natural variant4011R → S in MHS1. Ref.59
VAR_045707
Natural variant4021M → T in CFTD. Ref.67
VAR_063846
Natural variant4031I → M in CCD and MHS1. Ref.17 Ref.59
VAR_005593
Natural variant4711R → C. Ref.2
VAR_005594
Natural variant4851M → V. Ref.60
Corresponds to variant rs147723844 [ dbSNP | Ensembl ].
VAR_032911
Natural variant5221Y → S in CCD and MHS1. Ref.18 Ref.59
VAR_005595
Natural variant5301R → H in MHS1. Ref.65
VAR_058563
Natural variant5331R → C in MHS1. Ref.51
VAR_045708
Natural variant5331R → H in MHS1.
VAR_008971
Natural variant5441D → Y in MHS1. Ref.65
VAR_058564
Natural variant5521R → W in MHS1. Ref.24 Ref.59
VAR_005596
Natural variant6141R → C in CCD and MHS1; 3-5% of the cases. Ref.7 Ref.8 Ref.35 Ref.40 Ref.41 Ref.50 Ref.55 Ref.57 Ref.59
Corresponds to variant rs28933996 [ dbSNP | Ensembl ].
VAR_005597
Natural variant6141R → L in MHS1. Ref.23 Ref.59
VAR_005598
Natural variant10431R → C in MHS1. Ref.65
VAR_058565
Natural variant10581E → K in MHS1. Ref.66
VAR_068511
Natural variant10881Y → C Probable disease-associated mutation found in a family with Samaritan myopathy. Ref.16
VAR_068512
Natural variant11091R → K.
Corresponds to variant rs35719391 [ dbSNP | Ensembl ].
VAR_032912
Natural variant13421S → G. Ref.65
Corresponds to variant rs34694816 [ dbSNP | Ensembl ].
VAR_032913
Natural variant13521A → G in MHS1. Ref.65
Corresponds to variant rs112105381 [ dbSNP | Ensembl ].
VAR_058566
Natural variant13931K → R May be associated with susceptibility to malignant hyperthermia. Ref.66
Corresponds to variant rs137933390 [ dbSNP | Ensembl ].
VAR_068513
Natural variant14891S → N.
Corresponds to variant rs34404839 [ dbSNP | Ensembl ].
VAR_032914
Natural variant16791R → H May be associated with susceptibility to malignant hyperthermia. Ref.66
Corresponds to variant rs146504767 [ dbSNP | Ensembl ].
VAR_068514
Natural variant17041G → S in CCD; autosomal recessive form. Ref.64
VAR_045709
Natural variant17871P → L. Ref.2 Ref.65 Ref.68
Corresponds to variant rs34934920 [ dbSNP | Ensembl ].
VAR_005599
Natural variant18321G → A. Ref.4 Ref.46 Ref.65
VAR_045710
Natural variant20351H → L in CFTD. Ref.67
VAR_063847
Natural variant20601G → C. Ref.2 Ref.60 Ref.65 Ref.68
Corresponds to variant rs35364374 [ dbSNP | Ensembl ].
VAR_005600
Natural variant21011M → K. Ref.51
VAR_045711
Natural variant21171V → L in MHS1. Ref.51
VAR_045712
Natural variant21291D → E in MHS1. Ref.38 Ref.40
Corresponds to variant rs117886618 [ dbSNP | Ensembl ].
VAR_045713
Natural variant21631R → C in MHS1. Ref.25 Ref.55 Ref.59
Corresponds to variant rs28933998 [ dbSNP | Ensembl ].
VAR_005601
Natural variant21631R → H in CCD and MHS1. Ref.25 Ref.44 Ref.59
Corresponds to variant rs28933999 [ dbSNP | Ensembl ].
VAR_005602
Natural variant21631R → P in MHS1. Ref.51
VAR_008972
Natural variant21681V → M in CCD and MHS1; no difference in the thapsigargin-sensitive calcium stores of cells carrying this mutation and the wild-type. Ref.25 Ref.35 Ref.36 Ref.37 Ref.40 Ref.51 Ref.55 Ref.59
VAR_005603
Natural variant22041H → Q in CCD. Ref.68
Corresponds to variant rs141646642 [ dbSNP | Ensembl ].
VAR_068515
Natural variant22061T → M in MHS1; induces an increase sensitivity to caffeine. Ref.25 Ref.35 Ref.40 Ref.44 Ref.55 Ref.59
Corresponds to variant rs28934000 [ dbSNP | Ensembl ].
VAR_005604
Natural variant22061T → R in MHS1. Ref.59
VAR_008973
Natural variant22141V → I in MHS1. Ref.35 Ref.55
VAR_045714
Natural variant22801V → I in MHS1. Ref.44
VAR_045715
Natural variant23211I → V. Ref.65
Corresponds to variant rs34390345 [ dbSNP | Ensembl ].
VAR_058567
Natural variant23361R → H in MHS1. Ref.65
VAR_058568
Natural variant23421N → S in MHS1. Ref.58
Corresponds to variant rs147213895 [ dbSNP | Ensembl ].
VAR_045716
Natural variant23441E → D in MHS1; unknown pathological significance. Ref.59
VAR_045717
Natural variant23461V → M in MHS1. Ref.57 Ref.59
VAR_045718
Natural variant23471Missing in MHS1. Ref.34
VAR_045719
Natural variant23481E → G in MHS1. Ref.57
VAR_045720
Natural variant23501A → T in MHS1; reveals an altered calcium dependence and increased caffeine sensitivity. Ref.39 Ref.55 Ref.59
VAR_045721
Natural variant23551R → C in MHS1. Ref.45
VAR_045722
Natural variant23671A → T in MHS1. Ref.35 Ref.55
VAR_045723
Natural variant24041E → K in MHS1. Ref.65
VAR_058569
Natural variant24211A → P in CCD; autosomal recessive form. Ref.64
VAR_045724
Natural variant24231M → K in MMDO and CCD; autosomal recessive form. Ref.60 Ref.64
VAR_032915
Natural variant24281A → T in MHS1; induces an increase sensitivity to caffeine. Ref.40 Ref.59
VAR_045725
Natural variant24311D → N in MHS1. Ref.35 Ref.55
VAR_045726
Natural variant24341G → R in MHS1. Ref.20 Ref.21 Ref.35 Ref.40 Ref.44 Ref.55 Ref.59
VAR_005605
Natural variant24351R → H in CCD and MHS1. Ref.3 Ref.40 Ref.59
Corresponds to variant rs28933396 [ dbSNP | Ensembl ].
VAR_005606
Natural variant24351R → L in MHS1. Ref.28 Ref.44 Ref.51
VAR_008974
Natural variant24371A → V in MHS1. Ref.55
VAR_045727
Natural variant24521R → W in MHS1. Ref.30 Ref.40 Ref.57
VAR_045728
Natural variant24541R → C in MHS1; induces an increase sensitivity to caffeine. Ref.32 Ref.41 Ref.59
VAR_008975
Natural variant24541R → H in CCD and MHS1; severe form; induces an increase sensitivity to caffeine. Ref.28 Ref.30 Ref.35 Ref.40 Ref.51 Ref.55 Ref.59
VAR_008976
Natural variant24581R → C in MHS1. Ref.26 Ref.44 Ref.59
Corresponds to variant rs28933397 [ dbSNP | Ensembl ].
VAR_008977
Natural variant24581R → H in MHS1. Ref.26 Ref.57
VAR_008978
Natural variant25081R → G in CCD. Ref.66
VAR_068516
Natural variant25091V → I.
Corresponds to variant rs2071088 [ dbSNP | Ensembl ].
VAR_051891
Natural variant25501L → V. Ref.2 Ref.4 Ref.65
VAR_058570
Natural variant26761R → W in MHS1; located on the same allele as S-2787. Ref.56 Ref.59 Ref.65
Corresponds to variant rs28934001 [ dbSNP | Ensembl ].
VAR_045729
Natural variant27301D → G in MHS1. Ref.65
VAR_058571
Natural variant27791E → K.
Corresponds to variant rs2915952 [ dbSNP | Ensembl ].
VAR_051892
Natural variant27871T → S in MHS1; located on the same allele as W-2676. Ref.56 Ref.59 Ref.65
Corresponds to variant rs35180584 [ dbSNP | Ensembl ].
VAR_045730
Natural variant28801E → K in MHS1. Ref.65
VAR_058572
Natural variant31181A → V.
Corresponds to variant rs2915960 [ dbSNP | Ensembl ].
VAR_045731
Natural variant32171S → P in MHS1. Ref.65
VAR_058573
Natural variant32901E → K in MHS1. Ref.65
VAR_058574
Natural variant33261N → K in CFTD. Ref.67
VAR_063848
Natural variant33661R → H in CCD. Ref.68
Corresponds to variant rs137932199 [ dbSNP | Ensembl ].
VAR_068517
Natural variant34021C → G in CFTD. Ref.67
VAR_063849
Natural variant35271P → S in CCD; autosomal recessive form. Ref.42
VAR_045732
Natural variant35391R → H in CCD; autosomal recessive form. Ref.64
Corresponds to variant rs143987857 [ dbSNP | Ensembl ].
VAR_045733
Natural variant35831E → Q. Ref.65
Corresponds to variant rs55876273 [ dbSNP | Ensembl ].
VAR_058575
Natural variant37561Q → E. Ref.46 Ref.65
Corresponds to variant rs4802584 [ dbSNP | Ensembl ].
VAR_032916
Natural variant37721R → Q in CCD; autosomal recessive form. Ref.64
VAR_045734
Natural variant37721R → W in MHS1. Ref.65
VAR_058576
Natural variant38061G → R in MHS1. Ref.65
VAR_058577
Natural variant39161I → M in MHS1. Ref.41 Ref.59
VAR_045735
Natural variant39331Y → C in CCD. Ref.68
Corresponds to variant rs147136339 [ dbSNP | Ensembl ].
VAR_068518
Natural variant41361R → S in MHS1. Ref.44
VAR_045736
Natural variant4214 – 42163Missing in CCD.
VAR_045737
Natural variant42341V → L in MHS1. Ref.44
VAR_045738
Natural variant44931P → A. Ref.68
VAR_068519
Natural variant45011P → L in MHS1. Ref.65
Corresponds to variant rs73933023 [ dbSNP | Ensembl ].
VAR_058578
Natural variant45581R → Q in CCD; autosomal recessive form. Ref.62 Ref.64
VAR_045739
Natural variant46371T → A in CCD. Ref.33
VAR_045740
Natural variant46371T → I in core/rod disease. Ref.54
VAR_045741
Natural variant46381G → D in CCD. Ref.54 Ref.57
VAR_045742
Natural variant4647 – 46482Missing in CCD.
VAR_045743
Natural variant46501L → P in CCD; autosomal recessive form. Ref.50
VAR_045744
Natural variant46511H → P in CCD. Ref.54
VAR_045745
Natural variant46681P → S. Ref.46
VAR_045746
Natural variant46841F → S in MHS1. Ref.59
VAR_045747
Natural variant47241K → Q in CCD; autosomal recessive form. Ref.50
VAR_045748
Natural variant47371R → Q in MHS1. Ref.59
VAR_045749
Natural variant47371R → W in MHS1. Ref.44 Ref.59
VAR_045750
Natural variant47431G → D in CCD. Ref.68
VAR_068520
Natural variant47931L → P in CCD. Ref.36
VAR_045751
Natural variant47961Y → C in CCD. Ref.36
VAR_045752
Natural variant48141L → F in CCD. Ref.57
VAR_045753
Natural variant48241L → P in MHS1. Ref.55 Ref.57
VAR_045754
Natural variant48251R → C in CCD. Ref.36
VAR_045755
Natural variant48261T → I in MHS1. Ref.31 Ref.59
VAR_045756
Natural variant48381L → V in MHS1. Ref.46 Ref.59 Ref.65
VAR_045757
Natural variant48421V → M in CCD; autosomal recessive form. Ref.64
VAR_045758
Natural variant48461A → V in CCD; autosomal recessive form. Ref.61 Ref.62
VAR_045759
Natural variant48491V → I in MHS1 and CCD; autosomal recessive form. Ref.47 Ref.59 Ref.62 Ref.64
VAR_045760
Natural variant48601Missing in CCD. Ref.36
VAR_045761
Natural variant48611R → C in CCD. Ref.54 Ref.62
VAR_045762
Natural variant48611R → H in CCD; release of calcium from intracellular stores in the absence of any pharmacological activator of RYR; smaller thapsigargin-sensitive intracellular calcium stores; normal sensitivity of the calcium release to the RYR inhibitor dantrolene. Ref.36 Ref.37 Ref.49 Ref.54 Ref.57 Ref.62
VAR_045763
Natural variant4863 – 48697FYNKSED → Y in CCD.
VAR_045764
Natural variant48641Y → C in CCD. Ref.49
VAR_045765
Natural variant48761K → R in MHS1. Ref.59 Ref.65
VAR_045766
Natural variant48821T → M in CCD. Ref.63
VAR_068521
Natural variant48911G → R in CCD. Ref.37
VAR_045767
Natural variant48931R → Q in CCD. Ref.54
VAR_045768
Natural variant48931R → W in CCD; release of calcium from intracellular stores in the absence of any pharmacological activator of RYR; smaller thapsigargin-sensitive intracellular calcium stores; normal sensitivity of the calcium release to the RYR inhibitor dantrolene. Ref.36 Ref.37 Ref.49
VAR_045769
Natural variant48971G → V in CCD. Ref.62
VAR_045770
Natural variant48981I → T in CCD; severe phenotype; also present in some patients with MHS1; no response to the agonists halothane and caffeine. Ref.29 Ref.36 Ref.37 Ref.54
VAR_045771
Natural variant48991G → E in CCD. Ref.36 Ref.50
VAR_045772
Natural variant48991G → R in CCD; release of calcium from intracellular stores in the absence of any pharmacological activator of RYR; smaller thapsigargin-sensitive intracellular calcium stores; normal sensitivity of the calcium release to the RYR inhibitor dantrolene. Ref.37
VAR_045773
Natural variant49061A → V in CCD. Ref.37
VAR_045774
Natural variant49141R → G in CCD. Ref.36 Ref.54
VAR_045775
Natural variant49141R → T in CCD. Ref.54 Ref.62
VAR_045776
Natural variant4927 – 49282Missing in CCD.
VAR_045777
Natural variant49381I → M in CCD. Ref.57
VAR_045778
Natural variant49381I → T in MHS1. Ref.65
VAR_058579
Natural variant49391D → E in MHS1. Ref.57 Ref.59
VAR_045779
Natural variant49401A → T in CCD. Ref.49 Ref.54
VAR_045780
Natural variant49421G → V in MHS1. Ref.44
VAR_045781
Natural variant49731P → L in MHS1. Ref.41 Ref.44 Ref.59
VAR_045782

Experimental info

Sequence conflict1365 – 13684GEAQ → RGA AA sequence Ref.1
Sequence conflict23241N → K AA sequence Ref.1
Sequence conflict28401R → A AA sequence Ref.1
Sequence conflict33801R → A AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 13, 2006. Version 3.
Checksum: EC32277F4885CC7F

FASTA5,038565,176
        10         20         30         40         50         60 
MGDAEGEDEV QFLRTDDEVV LQCSATVLKE QLKLCLAAEG FGNRLCFLEP TSNAQNVPPD 

        70         80         90        100        110        120 
LAICCFVLEQ SLSVRALQEM LANTVEAGVE SSQGGGHRTL LYGHAILLRH AHSRMYLSCL 

       130        140        150        160        170        180 
TTSRSMTDKL AFDVGLQEDA TGEACWWTMH PASKQRSEGE KVRVGDDIIL VSVSSERYLH 

       190        200        210        220        230        240 
LSTASGELQV DASFMQTLWN MNPICSRCEE GFVTGGHVLR LFHGHMDECL TISPADSDDQ 

       250        260        270        280        290        300 
RRLVYYEGGA VCTHARSLWR LEPLRISWSG SHLRWGQPLR VRHVTTGQYL ALTEDQGLVV 

       310        320        330        340        350        360 
VDASKAHTKA TSFCFRISKE KLDVAPKRDV EGMGPPEIKY GESLCFVQHV ASGLWLTYAA 

       370        380        390        400        410        420 
PDPKALRLGV LKKKAMLHQE GHMDDALSLT RCQQEESQAA RMIHSTNGLY NQFIKSLDSF 

       430        440        450        460        470        480 
SGKPRGSGPP AGTALPIEGV ILSLQDLIIY FEPPSEDLQH EEKQSKLRSL RNRQSLFQEE 

       490        500        510        520        530        540 
GMLSMVLNCI DRLNVYTTAA HFAEFAGEEA AESWKEIVNL LYELLASLIR GNRSNCALFS 

       550        560        570        580        590        600 
TNLDWLVSKL DRLEASSGIL EVLYCVLIES PEVLNIIQEN HIKSIISLLD KHGRNHKVLD 

       610        620        630        640        650        660 
VLCSLCVCNG VAVRSNQDLI TENLLPGREL LLQTNLINYV TSIRPNIFVG RAEGTTQYSK 

       670        680        690        700        710        720 
WYFEVMVDEV TPFLTAQATH LRVGWALTEG YTPYPGAGEG WGGNGVGDDL YSYGFDGLHL 

       730        740        750        760        770        780 
WTGHVARPVT SPGQHLLAPE DVISCCLDLS VPSISFRING CPVQGVFESF NLDGLFFPVV 

       790        800        810        820        830        840 
SFSAGVKVRF LLGGRHGEFK FLPPPGYAPC HEAVLPRERL HLEPIKEYRR EGPRGPHLVG 

       850        860        870        880        890        900 
PSRCLSHTDF VPCPVDTVQI VLPPHLERIR EKLAENIHEL WALTRIEQGW TYGPVRDDNK 

       910        920        930        940        950        960 
RLHPCLVDFH SLPEPERNYN LQMSGETLKT LLALGCHVGM ADEKAEDNLK KTKLPKTYMM 

       970        980        990       1000       1010       1020 
SNGYKPAPLD LSHVRLTPAQ TTLVDRLAEN GHNVWARDRV GQGWSYSAVQ DIPARRNPRL 

      1030       1040       1050       1060       1070       1080 
VPYRLLDEAT KRSNRDSLCQ AVRTLLGYGY NIEPPDQEPS QVENQSRCDR VRIFRAEKSY 

      1090       1100       1110       1120       1130       1140 
TVQSGRWYFE FEAVTTGEMR VGWARPELRP DVELGADELA YVFNGHRGQR WHLGSEPFGR 

      1150       1160       1170       1180       1190       1200 
PWQPGDVVGC MIDLTENTII FTLNGEVLMS DSGSETAFRE IEIGDGFLPV CSLGPGQVGH 

      1210       1220       1230       1240       1250       1260 
LNLGQDVSSL RFFAICGLQE GFEPFAINMQ RPVTTWFSKG LPQFEPVPLE HPHYEVSRVD 

      1270       1280       1290       1300       1310       1320 
GTVDTPPCLR LTHRTWGSQN SLVEMLFLRL SLPVQFHQHF RCTAGATPLA PPGLQPPAED 

      1330       1340       1350       1360       1370       1380 
EARAAEPDPD YENLRRSAGG WSEAENGKEG TAKEGAPGGT PQAGGEAQPA RAENEKDATT 

      1390       1400       1410       1420       1430       1440 
EKNKKRGFLF KAKKVAMMTQ PPATPTLPRL PHDVVPADNR DDPEIILNTT TYYYSVRVFA 

      1450       1460       1470       1480       1490       1500 
GQEPSCVWAG WVTPDYHQHD MSFDLSKVRV VTVTMGDEQG NVHSSLKCSN CYMVWGGDFV 

      1510       1520       1530       1540       1550       1560 
SPGQQGRISH TDLVIGCLVD LATGLMTFTA NGKESNTFFQ VEPNTKLFPA VFVLPTHQNV 

      1570       1580       1590       1600       1610       1620 
IQFELGKQKN IMPLSAAMFQ SERKNPAPQC PPRLEMQMLM PVSWSRMPNH FLQVETRRAG 

      1630       1640       1650       1660       1670       1680 
ERLGWAVQCQ EPLTMMALHI PEENRCMDIL ELSERLDLQR FHSHTLRLYR AVCALGNNRV 

      1690       1700       1710       1720       1730       1740 
AHALCSHVDQ AQLLHALEDA HLPGPLRAGY YDLLISIHLE SACRSRRSML SEYIVPLTPE 

      1750       1760       1770       1780       1790       1800 
TRAITLFPPG RSTENGHPRH GLPGVGVTTS LRPPHHFSPP CFVAALPAAG AAEAPARLSP 

      1810       1820       1830       1840       1850       1860 
AIPLEALRDK ALRMLGEAVR DGGQHARDPV GGSVEFQFVP VLKLVSTLLV MGIFGDEDVK 

      1870       1880       1890       1900       1910       1920 
QILKMIEPEV FTEEEEEEDE EEEGEEEDEE EKEEDEEETA QEKEDEEKEE EEAAEGEKEE 

      1930       1940       1950       1960       1970       1980 
GLEEGLLQMK LPESVKLQMC HLLEYFCDQE LQHRVESLAA FAERYVDKLQ ANQRSRYGLL 

      1990       2000       2010       2020       2030       2040 
IKAFSMTAAE TARRTREFRS PPQEQINMLL QFKDGTDEED CPLPEEIRQD LLDFHQDLLA 

      2050       2060       2070       2080       2090       2100 
HCGIQLDGEE EEPEEETTLG SRLMSLLEKV RLVKKKEEKP EEERSAEESK PRSLQELVSH 

      2110       2120       2130       2140       2150       2160 
MVVRWAQEDF VQSPELVRAM FSLLHRQYDG LGELLRALPR AYTISPSSVE DTMSLLECLG 

      2170       2180       2190       2200       2210       2220 
QIRSLLIVQM GPQEENLMIQ SIGNIMNNKV FYQHPNLMRA LGMHETVMEV MVNVLGGGES 

      2230       2240       2250       2260       2270       2280 
KEIRFPKMVT SCCRFLCYFC RISRQNQRSM FDHLSYLLEN SGIGLGMQGS TPLDVAAASV 

      2290       2300       2310       2320       2330       2340 
IDNNELALAL QEQDLEKVVS YLAGCGLQSC PMLVAKGYPD IGWNPCGGER YLDFLRFAVF 

      2350       2360       2370       2380       2390       2400 
VNGESVEENA NVVVRLLIRK PECFGPALRG EGGSGLLAAI EEAIRISEDP ARDGPGIRRD 

      2410       2420       2430       2440       2450       2460 
RRREHFGEEP PEENRVHLGH AIMSFYAALI DLLGRCAPEM HLIQAGKGEA LRIRAILRSL 

      2470       2480       2490       2500       2510       2520 
VPLEDLVGII SLPLQIPTLG KDGALVQPKM SASFVPDHKA SMVLFLDRVY GIENQDFLLH 

      2530       2540       2550       2560       2570       2580 
VLDVGFLPDM RAAASLDTAT FSTTEMALAL NRYLCLAVLP LITKCAPLFA GTEHRAIMVD 

      2590       2600       2610       2620       2630       2640 
SMLHTVYRLS RGRSLTKAQR DVIEDCLMSL CRYIRPSMLQ HLLRRLVFDV PILNEFAKMP 

      2650       2660       2670       2680       2690       2700 
LKLLTNHYER CWKYYCLPTG WANFGVTSEE ELHLTRKLFW GIFDSLAHKK YDPELYRMAM 

      2710       2720       2730       2740       2750       2760 
PCLCAIAGAL PPDYVDASYS SKAEKKATVD AEGNFDPRPV ETLNVIIPEK LDSFINKFAE 

      2770       2780       2790       2800       2810       2820 
YTHEKWAFDK IQNNWSYGEN IDEELKTHPM LRPYKTFSEK DKEIYRWPIK ESLKAMIAWE 

      2830       2840       2850       2860       2870       2880 
WTIEKAREGE EEKTEKKKTR KISQSAQTYD PREGYNPQPP DLSAVTLSRE LQAMAEQLAE 

      2890       2900       2910       2920       2930       2940 
NYHNTWGRKK KQELEAKGGG THPLLVPYDT LTAKEKARDR EKAQELLKFL QMNGYAVTRG 

      2950       2960       2970       2980       2990       3000 
LKDMELDSSS IEKRFAFGFL QQLLRWMDIS QEFIAHLEAV VSSGRVEKSP HEQEIKFFAK 

      3010       3020       3030       3040       3050       3060 
ILLPLINQYF TNHCLYFLST PAKVLGSGGH ASNKEKEMIT SLFCKLAALV RHRVSLFGTD 

      3070       3080       3090       3100       3110       3120 
APAVVNCLHI LARSLDARTV MKSGPEIVKA GLRSFFESAS EDIEKMVENL RLGKVSQART 

      3130       3140       3150       3160       3170       3180 
QVKGVGQNLT YTTVALLPVL TTLFQHIAQH QFGDDVILDD VQVSCYRTLC SIYSLGTTKN 

      3190       3200       3210       3220       3230       3240 
TYVEKLRPAL GECLARLAAA MPVAFLEPQL NEYNACSVYT TKSPRERAIL GLPNSVEEMC 

      3250       3260       3270       3280       3290       3300 
PDIPVLERLM ADIGGLAESG ARYTEMPHVI EITLPMLCSY LPRWWERGPE APPSALPAGA 

      3310       3320       3330       3340       3350       3360 
PPPCTAVTSD HLNSLLGNIL RIIVNNLGID EASWMKRLAV FAQPIVSRAR PELLQSHFIP 

      3370       3380       3390       3400       3410       3420 
TIGRLRKRAG KVVSEEEQLR LEAKAEAQEG ELLVRDEFSV LCRDLYALYP LLIRYVDNNR 

      3430       3440       3450       3460       3470       3480 
AQWLTEPNPS AEELFRMVGE IFIYWSKSHN FKREEQNFVV QNEINNMSFL TADNKSKMAK 

      3490       3500       3510       3520       3530       3540 
AGDIQSGGSD QERTKKKRRG DRYSVQTSLI VATLKKMLPI GLNMCAPTDQ DLITLAKTRY 

      3550       3560       3570       3580       3590       3600 
ALKDTDEEVR EFLHNNLHLQ GKVEGSPSLR WQMALYRGVP GREEDADDPE KIVRRVQEVS 

      3610       3620       3630       3640       3650       3660 
AVLYYLDQTE HPYKSKKAVW HKLLSKQRRR AVVACFRMTP LYNLPTHRAC NMFLESYKAA 

      3670       3680       3690       3700       3710       3720 
WILTEDHSFE DRMIDDLSKA GEQEEEEEEV EEKKPDPLHQ LVLHFSRTAL TEKSKLDEDY 

      3730       3740       3750       3760       3770       3780 
LYMAYADIMA KSCHLEEGGE NGEAEEEVEV SFEEKQMEKQ RLLYQQARLH TRGAAEMVLQ 

      3790       3800       3810       3820       3830       3840 
MISACKGETG AMVSSTLKLG ISILNGGNAE VQQKMLDYLK DKKEVGFFQS IQALMQTCSV 

      3850       3860       3870       3880       3890       3900 
LDLNAFERQN KAEGLGMVNE DGTVINRQNG EKVMADDEFT QDLFRFLQLL CEGHNNDFQN 

      3910       3920       3930       3940       3950       3960 
YLRTQTGNTT TINIIICTVD YLLRLQESIS DFYWYYSGKD VIEEQGKRNF SKAMSVAKQV 

      3970       3980       3990       4000       4010       4020 
FNSLTEYIQG PCTGNQQSLA HSRLWDAVVG FLHVFAHMMM KLAQDSSQIE LLKELLDLQK 

      4030       4040       4050       4060       4070       4080 
DMVVMLLSLL EGNVVNGMIA RQMVDMLVES SSNVEMILKF FDMFLKLKDI VGSEAFQDYV 

      4090       4100       4110       4120       4130       4140 
TDPRGLISKK DFQKAMDSQK QFSGPEIQFL LSCSEADENE MINCEEFANR FQEPARDIGF 

      4150       4160       4170       4180       4190       4200 
NVAVLLTNLS EHVPHDPRLH NFLELAESIL EYFRPYLGRI EIMGASRRIE RIYFEISETN 

      4210       4220       4230       4240       4250       4260 
RAQWEMPQVK ESKRQFIFDV VNEGGEAEKM ELFVSFCEDT IFEMQIAAQI SEPEGEPETD 

      4270       4280       4290       4300       4310       4320 
EDEGAGAAEA GAEGAEEGAA GLEGTAATAA AGATARVVAA AGRALRGLSY RSLRRRVRRL 

      4330       4340       4350       4360       4370       4380 
RRLTAREAAT AVAALLWAAV TRAGAAGAGA AAGALGLLWG SLFGGGLVEG AKKVTVTELL 

      4390       4400       4410       4420       4430       4440 
AGMPDPTSDE VHGEQPAGPG GDADGEGASE GAGDAAEGAG DEEEAVHEAG PGGADGAVAV 

      4450       4460       4470       4480       4490       4500 
TDGGPFRPEG AGGLGDMGDT TPAEPPTPEG SPILKRKLGV DGVEEELPPE PEPEPEPELE 

      4510       4520       4530       4540       4550       4560 
PEKADAENGE KEEVPEPTPE PPKKQAPPSP PPKKEEAGGE FWGELEVQRV KFLNYLSRNF 

      4570       4580       4590       4600       4610       4620 
YTLRFLALFL AFAINFILLF YKVSDSPPGE DDMEGSAAGD VSGAGSGGSS GWGLGAGEEA 

      4630       4640       4650       4660       4670       4680 
EGDEDENMVY YFLEESTGYM EPALRCLSLL HTLVAFLCII GYNCLKVPLV IFKREKELAR 

      4690       4700       4710       4720       4730       4740 
KLEFDGLYIT EQPEDDDVKG QWDRLVLNTP SFPSNYWDKF VKRKVLDKHG DIYGRERIAE 

      4750       4760       4770       4780       4790       4800 
LLGMDLATLE ITAHNERKPN PPPGLLTWLM SIDVKYQIWK FGVIFTDNSF LYLGWYMVMS 

      4810       4820       4830       4840       4850       4860 
LLGHYNNFFF AAHLLDIAMG VKTLRTILSS VTHNGKQLVM TVGLLAVVVY LYTVVAFNFF 

      4870       4880       4890       4900       4910       4920 
RKFYNKSEDE DEPDMKCDDM MTCYLFHMYV GVRAGGGIGD EIEDPAGDEY ELYRVVFDIT 

      4930       4940       4950       4960       4970       4980 
FFFFVIVILL AIIQGLIIDA FGELRDQQEQ VKEDMETKCF ICGIGSDYFD TTPHGFETHT 

      4990       5000       5010       5020       5030 
LEEHNLANYM FFLMYLINKD ETEHTGQESY VWKMYQERCW DFFPAGDCFR KQYEDQLS 

« Hide

Isoform 2 [UniParc].

Checksum: 59C8B257F3ED6BF2
Show »

FASTA5,033564,691
Isoform 3 [UniParc].

Checksum: C2A4DBEA0FDEEE8B
Show »

FASTA5,033564,550

References

« Hide 'large scale' references
[1]"Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum."
Zorzato F., Fujii J., Otsu K., Phillips M.S., Green N.M., Lai F.A., Meissner G., Maclennan D.H.
J. Biol. Chem. 265:2244-2256(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
Tissue: Skeletal muscle.
[2]"Polymorphisms and deduced amino acid substitutions in the coding sequence of the ryanodine receptor (RYR1) gene in individuals with malignant hyperthermia."
Gillard E.F., Otsu K., Fujii J., Duff C.L., de Leon S., Khanna V.K., Britt B.A., Worton R.G., McLennan D.H.
Genomics 13:1247-1254(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 2324; 2840 AND 3380, VARIANT MHS1 ARG-248, VARIANTS CYS-471; LEU-1787; CYS-2060 AND VAL-2550.
Tissue: Muscle.
[3]"A mutation in the human ryanodine receptor gene associated with central core disease."
Zhang Y., Chen H.S., Khanna V.K., de Leon S., Phillips M.S., Schappert K.T., Britt B.A., Brownell A.K.W., McLennan D.H.
Nat. Genet. 5:46-50(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 1365-1368, VARIANT CCD/MHS1 HIS-2435, ALTERNATIVE SPLICING.
Tissue: Muscle.
[4]"The structural organization of the human skeletal muscle ryanodine receptor (RYR1) gene."
Phillips M.S., Fujii J., Khanna V.K., de Leon S., Yokobata K., de Jong P.J., McLennan D.H.
Genomics 34:24-41(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS ALA-1832 AND VAL-2550.
[5]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Refinement of diagnostic assays for a probable causal mutation for porcine and human malignant hyperthermia."
Otsu K., Phillips M.S., Khanna V.K., de Leon S., McLennan D.H.
Genomics 13:835-837(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 598-722.
Tissue: Skeletal muscle.
[7]"A substitution of cysteine for arginine 614 in the ryanodine receptor is potentially causative of human malignant hyperthermia."
Gillard E.F., Otsu K., Fujii J., Khanna V.K., de Leon S., Derdemezi J., Britt B.A., Duff C.L., Worton R.G., MacLennan D.H.
Genomics 11:751-755(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 603-641, VARIANT MHS1 CYS-614.
[8]"Ryanodine receptor gene point mutation and malignant hyperthermia susceptibility."
Moroni I., Gonano E.F., Comi G.P., Tegazzin V., Prelle A., Bordoni A., Bresolin N., Scarlato G.
J. Neurol. 242:127-133(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 603-627, VARIANT MHS1 CYS-614.
[9]"Isolation and partial cloning of ryanodine-sensitive Ca2+ release channel protein isoforms from human myometrial smooth muscle."
Lynn S., Morgan J.M., Lamb H.K., Meissner G., Gillespie J.I.
FEBS Lett. 372:6-12(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4696-4974.
Tissue: Myometrium.
[10]"Partial cloning and differential expression of ryanodine receptor/calcium-release channel genes in human tissues including the hippocampus and cerebellum."
Martin C., Chapman K.E., Seckl J.R., Ashley R.H.
Neuroscience 85:205-216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Cysteine-3635 is responsible for skeletal muscle ryanodine receptor modulation by NO."
Sun J., Xin C., Eu J.P., Stamler J.S., Meissner G.
Proc. Natl. Acad. Sci. U.S.A. 98:11158-11162(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-3635.
[12]"S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALM AND S100A1.
[13]"Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-2843, S-NITROSYLATION, IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; FKBP1A AND PROTEIN PHOSPHATASE 1.
[14]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-4864 AND SER-4867, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[15]"Ryanodine receptors: structure, expression, molecular details, and function in calcium release."
Lanner J.T., Georgiou D.K., Joshi A.D., Hamilton S.L.
Cold Spring Harb. Perspect. Biol. 2:E3996-E3996(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"Samaritan myopathy, an ultimately benign congenital myopathy, is caused by a RYR1 mutation."
Bohm J., Leshinsky-Silver E., Vassilopoulos S., Le Gras S., Lerman-Sagie T., Ginzberg M., Jost B., Lev D., Laporte J.
Acta Neuropathol. 124:575-581(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SAMARITAN MYOPATHY, VARIANT CYS-1088.
[17]"Mutations in the ryanodine receptor gene in central core disease and malignant hyperthermia."
Quane K.A., Healy J.M.S., Keating K.E., Manning B.M., Couch F.J., Palmucci L.M., Doriguzzi C., Fagerlund T.H., Berg K., Ording H., Bendixen D., Mortier W., Linz U., Muller C.R., McCarthy T.V.
Nat. Genet. 5:51-55(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD/MHS1 CYS-163 AND MET-403.
[18]"Mutation screening of the RYR1 gene in malignant hyperthermia: detection of a novel Tyr to Ser mutation in a pedigree with associated central cores."
Quane K.A., Keating K.E., Healy J.M.S., Manning B.M., Krivosic-Horber R., Krivosic I., Monnier N., Lunardi J., McCarthy T.V.
Genomics 23:236-239(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD/MHS1 SER-522.
[19]"Detection of a novel common mutation in the ryanodine receptor gene in malignant hyperthermia: implications for diagnosis and heterogeneity studies."
Quane K.A., Keating K.E., Manning B.M., Healy J.M.S., Monsieurs K., Heffron J.J.A., Lehane M., Heytens L., Krivosic-Horber R., Adnet P., Ellis F.R., Monnier N., Lunardi J., McCarthy T.V.
Hum. Mol. Genet. 3:471-476(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 ARG-341.
[20]"Detection of a novel RYR1 mutation in four malignant hyperthermia pedigrees."
Keating K.E., Quane K.A., Manning B.M., Lehane M., Hartung E., Censier K., Urwyler A., Klausnitzer M., Muller C.R., Heffron J.J.A., McCarthy T.V.
Hum. Mol. Genet. 3:1855-1858(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 ARG-2434.
[21]"The substitution of Arg for Gly2433 in the human skeletal muscle ryanodine receptor is associated with malignant hyperthermia."
Phillips M.S., Khanna V.K., de Leon S., Frodis W., Britt B.A., McLennan D.H.
Hum. Mol. Genet. 3:2181-2186(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 ARG-2434.
[22]"Identification of heterozygous and homozygous individuals with the novel RYR1 mutation Cys35Arg in a large kindred."
Lynch P.J., Krivosic-Horber R., Reyford H., Monnier N., Quane K.A., Adnet P., Haudecoeur G., Krivosic I., McCarthy T.V., Lunardi J.
Anesthesiology 86:620-626(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 ARG-35.
[23]"Detection of a novel mutation at amino acid position 614 in the ryanodine receptor in malignant hyperthermia."
Quane K.A., Ording H., Keating K.E., Manning B.M., Heine R., Bendixen D., Berg K., Krivosic-Horber R., Lehmann-Horn F., Fagerlund T.H., McCarthy T.V.
Br. J. Anaesth. 79:332-337(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 LEU-614.
[24]"Detection of a novel mutation in the ryanodine receptor gene in an Irish malignant hyperthermia pedigree: correlation of the IVCT response with the affected and unaffected haplotypes."
Keating K.E., Giblin L., Lynch P.J., Quane K.A., Lehane M., Heffron J.J.A., McCarthy T.V.
J. Med. Genet. 34:291-296(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 TRP-552.
[25]"Identification of novel mutations in the ryanodine-receptor gene (RYR1) in malignant hyperthermia: genotype-phenotype correlation."
Manning B.M., Quane K.A., Ording H., Urwyler A., Tegazzin V., Lehane M., O'Halloran J., Hartung E., Giblin L.M., Lynch P.J., Vaughan P., Censier K., Bendixen D., Comi G.P., Heytens L., Monsieurs K., Fagerlund T.H., Wolz W. expand/collapse author list , Heffron J.J.A., Mueller C.R., McCarthy T.V.
Am. J. Hum. Genet. 62:599-609(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-2163; MET-2168 AND MET-2206, VARIANT CCD/MHS1 HIS-2163.
[26]"Novel mutations at a CpG dinucleotide in the ryanodine receptor in malignant hyperthermia."
Manning B.M., Quane K.A., Lynch P.J., Urwyler A., Tegazzin V., Krivosic-Horber R., Censier K., Comi G.P., Adnet P., Wolz W., Lunardi J., Muller C.R., McCarthy T.V.
Hum. Mutat. 11:45-50(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-2458 AND HIS-2458.
[27]"Screening of the ryanodine receptor gene in 105 malignant hyperthermia families: novel mutations and concordance with the in vitro contracture test."
Brandt A., Schleithoff L., Jurkat-Rott K., Klingler W., Baur C., Lehmann-Horn F.
Hum. Mol. Genet. 8:2055-2062(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1.
[28]"Mutation screening of the RYR1 gene and identification of two novel mutations in Italian malignant hyperthermia families."
Barone V., Massa O., Intravaia E., Bracco A., Di Martino A., Tegazzin V., Cozzolino S., Sorrentino V.
J. Med. Genet. 36:115-118(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 LEU-2435, VARIANT CCD/MHS1 HIS-2454.
[29]"A mutation in the transmembrane/luminal domain of the ryanodine receptor is associated with abnormal Ca(2+) release channel function and severe central core disease."
Lynch P.J., Tong J., Lehane M., Mallet A., Giblin L., Heffron J.J.A., Vaughan P., Zafra G., MacLennan D.H., McCarthy T.V.
Proc. Natl. Acad. Sci. U.S.A. 96:4164-4169(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD THR-4898, CHARACTERIZATION OF VARIANT CCD THR-4898.
[30]"Malignant hyperthermia in infancy and identification of novel RYR1 mutation."
Chamley D., Pollock N.A., Stowell K.M., Brown R.L.
Br. J. Anaesth. 84:500-504(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 TRP-2452 AND HIS-2454.
[31]"A novel ryanodine receptor mutation and genotype-phenotype correlation in a large malignant hyperthermia New Zealand Maori pedigree."
Brown R.L., Pollock A.N., Couchman K.G., Hodges M., Hutchinson D.O., Waaka R., Lynch P., McCarthy T.V., Stowell K.M.
Hum. Mol. Genet. 9:1515-1524(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 ILE-4826.
[32]"Novel mutation in the RYR1 gene (R2454C) in a patient with malignant hyperthermia."
Gencik M., Gencik A., Mortier W., Epplen J.T.
Hum. Mutat. 15:122-122(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 CYS-2454.
[33]"A novel ryanodine receptor gene mutation causing both cores and rods in congenital myopathy."
Scacheri P.C., Hoffman E.P., Fratkin J.D., Semino-Mora C., Senchak A., Davis M.R., Laing N.G., Vedanarayanan V., Subramony S.H.
Neurology 55:1689-1696(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD ALA-4637.
[34]"Single-amino-acid deletion in the RYR1 gene, associated with malignant hyperthermia susceptibility and unusual contraction phenotype."
Sambuughin N., McWilliams S., de Bantel A., Sivakumar K., Nelson T.E.
Am. J. Hum. Genet. 69:204-208(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 GLU-2347 DEL.
[35]"North American malignant hyperthermia population: screening of the ryanodine receptor gene and identification of novel mutations."
Sambuughin N., Sei Y., Gallagher K.L., Wyre H.W., Madsen D., Nelson T.E., Fletcher J.E., Rosenberg H., Muldoon S.M.
Anesthesiology 95:594-599(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-163; ARG-248; CYS-614; MET-2168; MET-2206; ILE-2214; THR-2367; ASN-2431; ARG-2434 AND HIS-2454.
[36]"Familial and sporadic forms of central core disease are associated with mutations in the C-terminal domain of the skeletal muscle ryanodine receptor."
Monnier N., Romero N.B., Lerale J., Landrieu P., Nivoche Y., Fardeau M., Lunardi J.
Hum. Mol. Genet. 10:2581-2592(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD MET-2168; 4214-ARG--4216-PHE DEL; 4647-LEU-SER-4648 DEL; PRO-4793; CYS-4796; CYS-4825; PHE-4860 DEL; HIS-4861; TRP-4893; THR-4898; GLU-4899 AND GLY-4914.
[37]"Identification of four novel mutations in the C-terminal membrane spanning domain of the ryanodine receptor 1: association with central core disease and alteration of calcium homeostasis."
Tilgen N., Zorzato F., Halliger-Keller B., Muntoni F., Sewry C., Palmucci L.M., Schneider C., Hauser E., Lehmann-Horn F., Mueller C.R., Treves S.
Hum. Mol. Genet. 10:2879-2887(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD HIS-4861; ARG-4891; THR-4898; ARG-4899 AND VAL-4906, CHARACTERIZATION OF VARIANTS CCD MET-2168; HIS-4861; TRP-4893; THR-4898 AND ARG-4899.
[38]"Identification of a novel mutation in the ryanodine receptor gene (RYR1) in patients with malignant hyperthermia."
Rueffert H., Kraus H., Olthoff D., Deutrich C., Froster U.G.
Hum. Mutat. 17:238-238(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 GLU-2129.
[39]"Identification and functional characterization of a novel ryanodine receptor mutation causing malignant hyperthermia in North American and South American families."
Sambuughin N., Nelson T.E., Jankovic J., Xin C., Meissner G., Mullakandov M., Ji J., Rosenberg H., Sivakumar K., Goldfarb L.G.
Neuromuscul. Disord. 11:530-537(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 THR-2350, CHARACTERIZATION OF VARIANT MHS1 THR-2350.
[40]"Mutation screening in the ryanodine receptor 1 gene (RYR1) in patients susceptible to malignant hyperthermia who show definite IVCT results: identification of three novel mutations."
Rueffert H., Olthoff D., Deutrich C., Meinecke C.D., Froster U.G.
Acta Anaesthesiol. Scand. 46:692-698(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-163; ASN-166; ARG-341; HIS-401; CYS-614; GLU-2129; MET-2168; MET-2206; THR-2428; ARG-2434; HIS-2435; TRP-2452 AND HIS-2454.
[41]"Presence of two different genetic traits in malignant hyperthermia families: implication for genetic analysis, diagnosis, and incidence of malignant hyperthermia susceptibility."
Monnier N., Krivosic-Horber R., Payen J.-F., Kozak-Ribbens G., Nivoche Y., Adnet P., Reyford H., Lunardi J.
Anesthesiology 97:1067-1074(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-163; ARG-341; CYS-614; CYS-2454; MET-3916 AND LEU-4973.
[42]"A recessive form of central core disease, transiently presenting as multi-minicore disease, is associated with a homozygous mutation in the ryanodine receptor type 1 gene."
Ferreiro A., Monnier N., Romero N.B., Leroy J.-P., Boennemann C., Haenggeli C.-A., Straub V., Voss W.D., Nivoche Y., Jungbluth H., Lemainque A., Voit T., Lunardi J., Fardeau M., Guicheney P.
Ann. Neurol. 51:750-759(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD SER-3527.
[43]"Malignant hyperthermia associated with exercise-induced rhabdomyolysis or congenital abnormalities and a novel RYR1 mutation in New Zealand and Australian pedigrees."
Davis M., Brown R., Dickson A., Horton H., James D., Laing N., Marston R., Norgate M., Perlman D., Pollock N., Stowell K.
Br. J. Anaesth. 88:508-515(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 CYS-401.
[44]"Mutations in the RYR1 gene in Italian patients at risk for malignant hyperthermia: evidence for a cluster of novel mutations in the C-terminal region."
Galli L., Orrico A., Cozzolino S., Pietrini V., Tegazzin V., Sorrentino V.
Cell Calcium 32:143-151(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-163; CYS-401; HIS-2163; MET-2206; ILE-2280; ARG-2434; LEU-2435; CYS-2458; SER-4136; LEU-4234; TRP-4737; VAL-4942 AND LEU-4973.
[45]"Novel skeletal muscle ryanodine receptor mutation in a large Brazilian family with malignant hyperthermia."
McWilliams S., Nelson T., Sudo R.T., Zapata-Sudo G., Batti M., Sambuughin N.
Clin. Genet. 62:80-83(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 CYS-2355.
[46]"Novel mutations in C-terminal channel region of the ryanodine receptor in malignant hyperthermia patients."
Oyamada H., Oguchi K., Saitoh N., Yamazawa T., Hirose K., Kawana Y., Wakatsuki K., Oguchi K., Tagami M., Hanaoka K., Endo M., Iino M.
Jpn. J. Pharmacol. 88:159-166(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 VAL-4838, VARIANTS ALA-1832; GLU-3756 AND SER-4668.
[47]"Autosomal recessive inheritance of RYR1 mutations in a congenital myopathy with cores."
Jungbluth H., Muller C.R., Halliger-Keller B., Brockington M., Brown S.C., Feng L., Chattopadhyay A., Mercuri E., Manzur A.Y., Ferreiro A., Laing N.G., Davis M.R., Roper H.P., Dubowitz V., Bydder G., Sewry C.A., Muntoni F.
Neurology 59:284-287(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD ILE-4849.
[48]"Detection of a novel ryanodine receptor subtype 1 mutation (R328W) in a malignant hyperthermia family by sequencing of a leukocyte transcript."
Loke J.C.P., Kraev N., Sharma P., Du G., Patel L., Kraev A., MacLennan D.H.
Anesthesiology 99:297-302(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 TRP-328, CHARACTERIZATION OF VARIANT MHS1 TRP-328.
[49]"Central core disease: clinical, pathological, and genetic features."
Quinlivan R.M., Muller C.R., Davis M., Laing N.G., Evans G.A., Dwyer J., Dove J., Roberts A.P., Sewry C.A.
Arch. Dis. Child. 88:1051-1055(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD HIS-4861; CYS-4864; TRP-4893 AND THR-4940.
[50]"Dominant and recessive central core disease associated with RYR1 mutations and fetal akinesia."
Romero N.B., Monnier N., Viollet L., Cortey A., Chevallay M., Leroy J.P., Lunardi J., Fardeau M.
Brain 126:2341-2349(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD GLU-215; CYS-614; PRO-4650; GLN-4724 AND GLU-4899.
[51]"Scanning for mutations of the ryanodine receptor (RYR1) gene by denaturing HPLC: detection of three novel malignant hyperthermia alleles."
Tammaro A., Bracco A., Cozzolino S., Esposito M., Di Martino A., Savoia G., Zeuli L., Piluso G., Aurino S., Nigro V.
Clin. Chem. 49:761-768(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-44; CYS-533; LEU-2117; PRO-2163; MET-2168; LEU-2435 AND HIS-2454, VARIANT LYS-2101.
[52]"Clinical and functional effects of a deletion in a COOH-terminal lumenal loop of the skeletal muscle ryanodine receptor."
Zorzato F., Yamaguchi N., Xu L., Meissner G., Mueller C.R., Pouliquin P., Muntoni F., Sewry C., Girard T., Treves S.
Hum. Mol. Genet. 12:379-388(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD 4863-ARG--ASP-4869 DELINS TYR.
[53]"A homozygous splicing mutation causing a depletion of skeletal muscle RYR1 is associated with multi-minicore disease congenital myopathy with ophthalmoplegia."
Monnier N., Ferreiro A., Marty I., Labarre-Vila A., Mezin P., Lunardi J.
Hum. Mol. Genet. 12:1171-1178(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MMDO.
[54]"Principal mutation hotspot for central core disease and related myopathies in the C-terminal transmembrane region of the RYR1 gene."
Davis M.R., Haan E., Jungbluth H., Sewry C., North K., Muntoni F., Kuntzer T., Lamont P., Bankier A., Tomlinson P., Sanchez A., Walsh P., Nagarajan L., Oley C., Colley A., Gedeon A., Quinlivan R., Dixon J. expand/collapse author list , James D., Mueller C.R., Laing N.G.
Neuromuscul. Disord. 13:151-157(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CORE/ROD DISEASE ILE-4637, VARIANTS CCD ASP-4638; PRO-4651; CYS-4861; HIS-4861; GLN-4893; THR-4898; GLY-4914; THR-4914; 4927-VAL-ILE-4928 DEL AND THR-4940.
[55]"Malignant hyperthermia in North America: genetic screening of the three hot spots in the type I ryanodine receptor gene."
Sei Y., Sambuughin N.N., Davis E.J., Sachs D., Cuenca P.B., Brandom B.W., Tautz T., Rosenberg H., Nelson T.E., Muldoon S.M.
Anesthesiology 101:824-830(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 CYS-163; ARG-248; CYS-614; CYS-2163; MET-2168; MET-2206; ILE-2214; THR-2350; THR-2367; ASN-2431; ARG-2434; VAL-2437; HIS-2454 AND PRO-4824.
[56]"Multiminicore disease in a family susceptible to malignant hyperthermia: histology, in vitro contracture tests, and genetic characterization."
Guis S., Figarella-Branger D., Monnier N., Bendahan D., Kozak-Ribbens G., Mattei J.-P., Lunardi J., Cozzone P.J., Pellissier J.-F.
Arch. Neurol. 61:106-113(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 TRP-2676 AND SER-2787.
[57]"RYR1 mutations in UK central core disease patients: more than just the C-terminal transmembrane region of the RYR1 gene."
Shepherd S., Ellis F., Halsall J., Hopkins P., Robinson R.
J. Med. Genet. 41:E33-E33(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD GLY-160; ASP-4638; PHE-4814; HIS-4861 AND MET-4938, VARIANTS MHS1 CYS-614; MET-2346; GLY-2348; TRP-2452; HIS-2458; PRO-4824 AND GLU-4939.
[58]"Mutation analysis of two patients with hypokalemic periodic paralysis and suspected malignant hyperthermia."
Marchant C.L., Ellis F.R., Halsall P.J., Hopkins P.M., Robinson R.L.
Muscle Nerve 30:114-117(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MHS1 SER-2342.
[59]"Correlations between genotype and pharmacological, histological, functional, and clinical phenotypes in malignant hyperthermia susceptibility."
Monnier N., Kozak-Ribbens G., Krivosic-Horber R., Nivoche Y., Qi D., Kraev N., Loke J., Sharma P., Tegazzin V., Figarella-Branger D., Romero N., Mezin P., Bendahan D., Payen J.-F., Depret T., Maclennan D.H., Lunardi J.
Hum. Mutat. 26:413-425(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 ARG-35; CYS-163; LEU-163; ARG-165; ASN-166; CYS-177; CYS-178; VAL-227; ARG-248; TRP-328; ARG-341; SER-401; HIS-401; MET-403; SER-522; TRP-552; CYS-614; LEU-614; CYS-2163; HIS-2163; MET-2168; MET-2206; ARG-2206; ASP-2344; MET-2346; THR-2350; THR-2428; ARG-2434; HIS-2435; CYS-2454; HIS-2454; CYS-2458; TRP-2676; SER-2787; MET-3916; SER-4684; GLN-4737; TRP-4737; ILE-4826; VAL-4838; ILE-4849; ARG-4876; GLU-4939 AND LEU-4973, CHARACTERIZATION OF VARIANTS MHS1 LEU-163; MET-2206; THR-2428; CYS-2454 AND HIS-2454.
[60]"Minicore myopathy with ophthalmoplegia caused by mutations in the ryanodine receptor type 1 gene."
Jungbluth H., Zhou H., Hartley L., Halliger-Keller B., Messina S., Longman C., Brockington M., Robb S.A., Straub V., Voit T., Swash M., Ferreiro A., Bydder G., Sewry C.A., Mueller C., Muntoni F.
Neurology 65:1930-1935(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MMDO TRP-109 AND LYS-2423, VARIANTS VAL-485 AND CYS-2060.
[61]"Inheritance of a novel RYR1 mutation in a family with myotonic dystrophy type 1."
Gambelli S., Malandrini A., Berti G., Gaudiano C., Zicari E., Brunori P., Perticoni G., Orrico A., Galli L., Sorrentino V., Lunardi J., Federico A., Dotti M.T.
Clin. Genet. 71:93-94(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD VAL-4846.
[62]"Central core disease due to recessive mutations in RYR1 gene: is it more common than described?"
Kossugue P.M., Paim J.F., Navarro M.M., Silva H.C., Pavanello R.C.M., Gurgel-Giannetti J., Zatz M., Vainzof M.
Muscle Nerve 35:670-674(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD GLN-4558; VAL-4846; ILE-4849; HIS-4861; CYS-4861; VAL-4897 AND THR-4914.
[63]"Novel RYR1 missense mutation causes core rod myopathy."
von der Hagen M., Kress W., Hahn G., Brocke K.S., Mitzscherling P., Huebner A., Muller-Reible C., Stoltenburg-Didinger G., Kaindl A.M.
Eur. J. Neurol. 15:E31-E32(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CCD MET-4882.
[64]"Null mutations causing depletion of the type 1 ryanodine receptor (RYR1) are commonly associated with recessive structural congenital myopathies with cores."
Monnier N., Marty I., Faure J., Castiglioni C., Desnuelle C., Sacconi S., Estournet B., Ferreiro A., Romero N., Laquerriere A., Lazaro L., Martin J.-J., Morava E., Rossi A., Van der Kooi A., de Visser M., Verschuuren C., Lunardi J.
Hum. Mutat. 29:670-678(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD VAL-13; SER-1704; PRO-2421; LYS-2423; HIS-3539; GLN-3772; GLN-4558; MET-4842 AND ILE-4849.
[65]"Increasing the number of diagnostic mutations in malignant hyperthermia."
Levano S., Vukcevic M., Singer M., Matter A., Treves S., Urwyler A., Girard T.
Hum. Mutat. 30:590-598(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 ARG-13; LYS-226; LEU-367; HIS-530; TYR-544; CYS-1043; GLY-1352; HIS-2336; LYS-2404; TRP-2676; GLY-2730; SER-2787; LYS-2880; PRO-3217; LYS-3290; TRP-3772; ARG-3806; LEU-4501; VAL-4838; ARG-4876 AND THR-4938, VARIANTS GLY-1342; LEU-1787; ALA-1832; CYS-2060; VAL-2321; VAL-2550; GLN-3583 AND GLU-3756.
[66]"Functional properties of RYR1 mutations identified in Swedish patients with malignant hyperthermia and central core disease."
Vukcevic M., Broman M., Islander G., Bodelsson M., Ranklev-Twetman E., Muller C.R., Treves S.
Anesth. Analg. 111:185-190(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MHS1 ASN-382 AND LYS-1058, VARIANT CCD GLY-2508, VARIANTS ARG-1393 AND HIS-1679.
[67]"Recessive mutations in RYR1 are a common cause of congenital fiber type disproportion."
Clarke N.F., Waddell L.B., Cooper S.T., Perry M., Smith R.L.L., Kornberg A.J., Muntoni F., Lillis S., Straub V., Bushby K., Guglieri M., King M.D., Farrell M.A., Marty I., Lunardi J., Monnier N., North K.N.
Hum. Mutat. 31:E1544-E1550(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CFTD THR-402; LEU-2035; LYS-3326 AND GLY-3402.
[68]"Dominant and recessive RYR1 mutations in adults with core lesions and mild muscle symptoms."
Duarte S.T., Oliveira J., Santos R., Pereira P., Barroso C., Conceicao I., Evangelista T.
Muscle Nerve 44:102-108(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CCD GLY-160; GLN-2204; HIS-3366; CYS-3933 AND ASP-4743, VARIANTS LEU-1787; CYS-2060 AND ALA-4493.
+Additional computationally mapped references.

Web resources

Wikipedia

Ryanodine receptor entry

Wikipedia

RYR1 entry

Leiden Muscular Dystrophy pages Ryanodine receptor 1 (skeletal) (RYR1)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05200 mRNA. Translation: AAA60294.1.
U48508 expand/collapse EMBL AC list , U48449, U48450, U48451, U48452, U48453, U48454, U48455, U48456, U48457, U48458, U48459, U48460, U48461, U48462, U48463, U48464, U48465, U48466, U48467, U48468, U48469, U48470, U48471, U48472, U48473, U48474, U48475, U48476, U48477, U48478, U48479, U48480, U48481, U48482, U48483, U48484, U48485, U48486, U48487, U48488, U48489, U48490, U48491, U48492, U48493, U48494, U48495, U48496, U48497, U48498, U48499, U48500, U48501, U48502, U48503, U48504, U48505, U48506, U48507 Genomic DNA. Translation: AAC51191.1.
AC067969 Genomic DNA. Translation: AAF66076.1.
AC005933 Genomic DNA. Translation: AAC71651.1.
AC011469 Genomic DNA. No translation available.
M91455 Genomic DNA. Translation: AAA60295.1.
S78717 Genomic DNA. Translation: AAB21245.2.
S77392 Genomic DNA. Translation: AAB34356.1.
CCDSCCDS33011.1. [P21817-1]
CCDS42563.1. [P21817-2]
PIRA35041.
RefSeqNP_000531.2. NM_000540.2. [P21817-1]
NP_001036188.1. NM_001042723.1. [P21817-2]
UniGeneHs.466664.

3D structure databases

ProteinModelPortalP21817.
SMRP21817. Positions 11-533, 849-1056, 2734-2940, 3614-3640, 4074-4131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112173. 8 interactions.
DIPDIP-29708N.
IntActP21817. 10 interactions.
MINTMINT-1605046.
STRING9606.ENSP00000352608.

Chemistry

BindingDBP21817.
ChEMBLCHEMBL1846.
DrugBankDB01219. Dantrolene.
GuidetoPHARMACOLOGY747.

Protein family/group databases

TCDB1.A.3.1.2. the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.

PTM databases

PhosphoSiteP21817.

Polymorphism databases

DMDM108935904.

Proteomic databases

PaxDbP21817.
PRIDEP21817.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355481; ENSP00000347667; ENSG00000196218. [P21817-2]
ENST00000359596; ENSP00000352608; ENSG00000196218. [P21817-1]
ENST00000360985; ENSP00000354254; ENSG00000196218. [P21817-3]
GeneID6261.
KEGGhsa:6261.
UCSCuc002oit.3. human. [P21817-1]
uc002oiu.3. human. [P21817-2]

Organism-specific databases

CTD6261.
GeneCardsGC19P038924.
GeneReviewsRYR1.
H-InvDBHIX0039957.
HGNCHGNC:10483. RYR1.
HPAHPA056416.
MIM117000. phenotype.
145600. phenotype.
180901. gene.
255310. phenotype.
255320. phenotype.
neXtProtNX_P21817.
Orphanet169189. Autosomal dominant centronuclear myopathy.
324581. Benign Samaritan congenital myopathy.
597. Central core disease.
98905. Congenital multicore myopathy with external ophthalmoplegia.
99741. King-Denborough syndrome.
423. Malignant hyperthermia.
178145. Moderate multiminicore disease with hand involvement.
PharmGKBPA34896.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247670.
HOGENOMHOG000231428.
HOVERGENHBG006699.
InParanoidP21817.
KOK04961.
OMAQCSATVL.
OrthoDBEOG71K622.
PhylomeDBP21817.
TreeFamTF315244.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP21817.
BgeeP21817.
CleanExHS_RYR1.
GenevestigatorP21817.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR011992. EF-hand-dom_pair.
IPR014821. Ins145_P3_rcpt.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR013333. Ryan_recept.
IPR003032. Ryanodine_rcpt.
IPR015925. Ryanodine_recept-rel.
IPR009460. Ryanrecept_TM4-6.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF06459. RR_TM4-6. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
PF02026. RyR. 4 hits.
PF00622. SPRY. 3 hits.
[Graphical view]
PRINTSPR00795. RYANODINER.
SMARTSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRYR1.
GenomeRNAi6261.
NextBio24319.
PROP21817.
SOURCESearch...

Entry information

Entry nameRYR1_HUMAN
AccessionPrimary (citable) accession number: P21817
Secondary accession number(s): Q16314 expand/collapse secondary AC list , Q16368, Q9NPK1, Q9P1U4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: June 13, 2006
Last modified: July 9, 2014
This is version 170 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM