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Q92736 - RYR2_HUMAN

UniProt

Q92736 - RYR2_HUMAN

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Protein

Ryanodine receptor 2

Gene

RYR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca2+ levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development.2 Publications

GO - Molecular functioni

  1. calcium channel activity Source: UniProtKB
  2. calcium-induced calcium release activity Source: BHF-UCL
  3. calcium ion binding Source: InterPro
  4. calcium-release channel activity Source: BHF-UCL
  5. calmodulin binding Source: BHF-UCL
  6. enzyme binding Source: BHF-UCL
  7. identical protein binding Source: BHF-UCL
  8. intracellular ligand-gated calcium channel activity Source: UniProtKB
  9. ion channel binding Source: BHF-UCL
  10. protein kinase A catalytic subunit binding Source: BHF-UCL
  11. protein kinase A regulatory subunit binding Source: BHF-UCL
  12. ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  13. suramin binding Source: BHF-UCL

GO - Biological processi

  1. BMP signaling pathway Source: Ensembl
  2. calcium ion transport Source: BHF-UCL
  3. calcium ion transport into cytosol Source: BHF-UCL
  4. calcium-mediated signaling Source: UniProtKB
  5. calcium-mediated signaling using intracellular calcium source Source: BHF-UCL
  6. canonical Wnt signaling pathway Source: Ensembl
  7. cardiac muscle contraction Source: BHF-UCL
  8. cardiac muscle hypertrophy Source: BHF-UCL
  9. cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
  10. cellular calcium ion homeostasis Source: UniProtKB
  11. cellular response to caffeine Source: UniProtKB
  12. cellular response to epinephrine stimulus Source: BHF-UCL
  13. cytosolic calcium ion homeostasis Source: BHF-UCL
  14. detection of calcium ion Source: BHF-UCL
  15. embryonic heart tube morphogenesis Source: UniProtKB
  16. establishment of protein localization to endoplasmic reticulum Source: BHF-UCL
  17. ion transmembrane transport Source: Reactome
  18. left ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
  19. positive regulation of calcium-transporting ATPase activity Source: BHF-UCL
  20. positive regulation of heart rate Source: BHF-UCL
  21. positive regulation of ryanodine-sensitive calcium-release channel activity by adrenergic receptor signaling pathway involved in positive regulation of cardiac muscle contraction Source: BHF-UCL
  22. positive regulation of sequestering of calcium ion Source: BHF-UCL
  23. positive regulation of the force of heart contraction Source: BHF-UCL
  24. Purkinje myocyte to ventricular cardiac muscle cell signaling Source: BHF-UCL
  25. regulation of cardiac muscle contraction Source: BHF-UCL
  26. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  27. regulation of heart rate Source: BHF-UCL
  28. release of sequestered calcium ion into cytosol Source: BHF-UCL
  29. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  30. response to caffeine Source: BHF-UCL
  31. response to hypoxia Source: BHF-UCL
  32. response to muscle stretch Source: BHF-UCL
  33. response to redox state Source: BHF-UCL
  34. sarcoplasmic reticulum calcium ion transport Source: BHF-UCL
  35. transmembrane transport Source: Reactome
  36. type B pancreatic cell apoptotic process Source: BHF-UCL
  37. ventricular cardiac muscle cell action potential Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Developmental protein, Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.

Protein family/group databases

TCDBi1.A.3.1.1. the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ryanodine receptor 2
Short name:
RYR-2
Short name:
RyR2
Short name:
hRYR-2
Alternative name(s):
Cardiac muscle ryanodine receptor
Cardiac muscle ryanodine receptor-calcium release channel
Type 2 ryanodine receptor
Gene namesi
Name:RYR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10484. RYR2.

Subcellular locationi

Sarcoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 42814281CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei4282 – 430221HelicalSequence AnalysisAdd
BLAST
Transmembranei4504 – 452421HelicalSequence AnalysisAdd
BLAST
Transmembranei4580 – 460021HelicalSequence AnalysisAdd
BLAST
Transmembranei4730 – 475021HelicalSequence AnalysisAdd
BLAST
Transmembranei4769 – 478921HelicalSequence AnalysisAdd
BLAST
Intramembranei4820 – 482910Pore-formingBy similarity
Transmembranei4850 – 487021HelicalSequence AnalysisAdd
BLAST
Topological domaini4871 – 496797CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. calcium channel complex Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProtKB
  3. junctional sarcoplasmic reticulum membrane Source: BHF-UCL
  4. membrane Source: BHF-UCL
  5. plasma membrane Source: BHF-UCL
  6. protein complex Source: MGI
  7. sarcoplasmic reticulum Source: BHF-UCL
  8. sarcoplasmic reticulum membrane Source: BHF-UCL
  9. smooth endoplasmic reticulum Source: Ensembl
  10. Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Arrhythmogenic right ventricular dysplasia, familial, 21 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA congenital heart disease characterized by infiltration of adipose and fibrous tissue into the right ventricle and loss of myocardial cells, resulting in ventricular and supraventricular arrhythmias.

See also OMIM:600996
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti176 – 1761R → Q in ARVD2 and CPVT1. 2 Publications
VAR_044087
Natural varianti433 – 4331L → P in ARVD2 and CPVT1. 2 Publications
VAR_011395
Natural varianti2386 – 23861N → I in ARVD2 and CPVT1. 2 Publications
VAR_011398
Natural varianti2504 – 25041T → M in ARVD2 and CPVT1. 2 Publications
VAR_044096
Ventricular tachycardia, catecholaminergic polymorphic, 1, with or without atrial dysfunction and/or dilated cardiomyopathy7 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress.

See also OMIM:604772
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641P → S in CPVT1. 1 Publication
VAR_044086
Natural varianti176 – 1761R → Q in ARVD2 and CPVT1. 2 Publications
VAR_044087
Natural varianti414 – 4141R → L in CPVT1. 1 Publication
VAR_044088
Natural varianti419 – 4191I → F in CPVT1. 1 Publication
VAR_044089
Natural varianti420 – 4201R → W in CPVT1. 2 Publications
Corresponds to variant rs190140598 [ dbSNP | Ensembl ].		VAR_044090
Natural varianti433 – 4331L → P in ARVD2 and CPVT1. 2 Publications
VAR_011395
Natural varianti2246 – 22461S → L in CPVT1. 3 Publications
VAR_011396
Natural varianti2306 – 23061V → I in CPVT1. 1 Publication
VAR_023694
Natural varianti2311 – 23111E → D in CPVT1. 1 Publication
VAR_044092
Natural varianti2328 – 23281P → S in CPVT1. 1 Publication
VAR_011397
Natural varianti2386 – 23861N → I in ARVD2 and CPVT1. 2 Publications
VAR_011398
Natural varianti2387 – 23871A → P in CPVT1. 1 Publication
VAR_044093
Natural varianti2392 – 23921Y → C in CPVT1. 1 Publication
VAR_044094
Natural varianti2403 – 24031A → T in CPVT1. 1 Publication
VAR_044095
Natural varianti2474 – 24741R → S in CPVT1. 2 Publications
VAR_011399
Natural varianti2504 – 25041T → M in ARVD2 and CPVT1. 2 Publications
VAR_044096
Natural varianti3778 – 37781L → F in CPVT1. 1 Publication
VAR_044097
Natural varianti3946 – 39461G → S in CPVT1. 1 Publication
VAR_044098
Natural varianti4097 – 40971N → S in CPVT1. 1 Publication
VAR_044099
Natural varianti4104 – 41041N → K in CPVT1. 2 Publications
VAR_011400
Natural varianti4146 – 41461E → K in CPVT1. 1 Publication
VAR_044100
Natural varianti4158 – 41581T → P in CPVT1. 1 Publication
VAR_044101
Natural varianti4201 – 42011Q → R in CPVT1. 1 Publication
VAR_011401
Natural varianti4497 – 44971R → C in CPVT1. 3 Publications
VAR_011402
Natural varianti4499 – 44991F → C in CPVT1. 1 Publication
VAR_044102
Natural varianti4504 – 45041M → I in CPVT1. 1 Publication
VAR_044103
Natural varianti4510 – 45101A → T in CPVT1. 1 Publication
VAR_044104
Natural varianti4607 – 46071A → P in CPVT1. 1 Publication
VAR_044105
Natural varianti4653 – 46531V → F in CPVT1. 1 Publication
VAR_011403
Natural varianti4671 – 46711G → R in CPVT1. 1 Publication
VAR_044106
Natural varianti4771 – 47711V → I in CPVT1. 1 Publication
VAR_044107
Natural varianti4848 – 48481I → V in CPVT1. 1 Publication
VAR_044108
Natural varianti4860 – 48601A → G in CPVT1; diminishes the response to activation by luminal Ca(2+) but has little effect on the sensitivity of the channel to activation by cytosolic Ca(2+); shows caffeine-induced Ca(2+) release but exhibits no store-overload-induced Ca(2+) release (SOICR); HL1 cardiac cells transfected with the G-4860 mutant displayed attenuated SOICR activity compared to cells transfected with wild-type RYR2. 2 Publications
VAR_044109
Natural varianti4867 – 48671I → M in CPVT1. 1 Publication
VAR_044110
Natural varianti4880 – 48801V → A in CPVT1. 1 Publication
VAR_044111
Natural varianti4895 – 48951N → D in CPVT1. 1 Publication
VAR_044112
Natural varianti4902 – 49021P → L in CPVT1. 1 Publication
VAR_023695
Natural varianti4950 – 49501E → K in CPVT1. 1 Publication
VAR_044113
Natural varianti4959 – 49591R → Q in CPVT1. 1 Publication
VAR_023696

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2808 – 28081S → A: Abolishes phosphorylation by PKA. 1 Publication

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi600996. phenotype.
604772. phenotype.
Orphaneti3286. Catecholaminergic polymorphic ventricular tachycardia.
293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 49674967Ryanodine receptor 2PRO_0000219361Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2031 – 20311Phosphoserine; by PKABy similarity
Modified residuei2808 – 28081Phosphoserine; by CaMK2D and PKA2 Publications
Modified residuei2814 – 28141Phosphoserine; by CaMK2D1 Publication

Post-translational modificationi

Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2808 and Ser-2814 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca2+ levels.2 Publications
Phosphorylation at Ser-2031 by PKA enhances the response to lumenal calcium.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92736.
PaxDbiQ92736.
PRIDEiQ92736.

PTM databases

PhosphoSiteiQ92736.

Expressioni

Tissue specificityi

Detected in heart muscle (at protein level). Heart muscle, brain (cerebellum and hippocampus) and placenta.2 Publications

Developmental stagei

Expressed in myometrium during pregnancy.1 Publication

Inductioni

By TGFB1.1 Publication

Gene expression databases

BgeeiQ92736.
CleanExiHS_RYR2.
ExpressionAtlasiQ92736. baseline and differential.
GenevestigatoriQ92736.

Organism-specific databases

HPAiCAB006834.
HPA016697.
HPA020028.

Interactioni

Subunit structurei

Homotetramer. Can also form heterotetramers with RYR1 and RYR3 (By similarity). Interacts with FKBP1A and FKBP1B; these interactions may stabilize the channel in its closed state and prevent Ca2+ leaks. Interacts with CALM and S100A1; these interactions regulate channel activity. Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with FKBP1B, PKA, PP1 and PP2A.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP1BP681062EBI-1170425,EBI-6693977
MDM2Q009872EBI-1170425,EBI-389668

Protein-protein interaction databases

BioGridi112174. 25 interactions.
DIPiDIP-38325N.
IntActiQ92736. 9 interactions.
MINTiMINT-1201008.
STRINGi9606.ENSP00000355533.

Structurei

Secondary structure

1
4967
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 2810Combined sources
Beta strandi31 – 388Combined sources
Beta strandi48 – 514Combined sources
Turni53 – 575Combined sources
Helixi63 – 653Combined sources
Beta strandi67 – 737Combined sources
Turni108 – 1103Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi129 – 1324Combined sources
Turni139 – 1413Combined sources
Beta strandi145 – 1517Combined sources
Beta strandi159 – 1668Combined sources
Beta strandi180 – 1856Combined sources
Turni186 – 1883Combined sources
Beta strandi191 – 1966Combined sources
Beta strandi198 – 20811Combined sources
Beta strandi212 – 2187Combined sources
Beta strandi233 – 2386Combined sources
Turni239 – 2424Combined sources
Beta strandi243 – 2464Combined sources
Beta strandi250 – 2523Combined sources
Helixi256 – 2583Combined sources
Beta strandi261 – 2633Combined sources
Helixi265 – 2695Combined sources
Helixi271 – 2733Combined sources
Beta strandi275 – 2806Combined sources
Turni283 – 2864Combined sources
Beta strandi295 – 2995Combined sources
Turni300 – 3023Combined sources
Beta strandi305 – 3084Combined sources
Beta strandi310 – 3123Combined sources
Beta strandi314 – 3174Combined sources
Helixi319 – 3213Combined sources
Helixi324 – 3274Combined sources
Beta strandi329 – 3368Combined sources
Beta strandi340 – 3423Combined sources
Turni356 – 3583Combined sources
Beta strandi360 – 3656Combined sources
Turni366 – 3683Combined sources
Beta strandi371 – 3755Combined sources
Beta strandi388 – 3969Combined sources
Beta strandi403 – 4075Combined sources
Helixi410 – 43728Combined sources
Helixi442 – 4443Combined sources
Helixi449 – 46214Combined sources
Helixi472 – 49120Combined sources
Helixi494 – 50613Combined sources
Beta strandi508 – 5103Combined sources
Helixi511 – 5188Combined sources
Helixi520 – 54122Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JKQX-ray2.39A1-606[»]
ProteinModelPortaliQ92736.
SMRiQ92736. Positions 10-544, 862-1068, 1082-1218, 2701-2905, 3581-3607, 4030-4086.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 16556MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini172 – 21746MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini225 – 28056MIR 3PROSITE-ProRule annotationAdd
BLAST
Domaini286 – 34358MIR 4PROSITE-ProRule annotationAdd
BLAST
Domaini351 – 40858MIR 5PROSITE-ProRule annotationAdd
BLAST
Domaini599 – 809211B30.2/SPRY 1PROSITE-ProRule annotationAdd
BLAST
Repeati853 – 9661141Add
BLAST
Repeati967 – 10801142Add
BLAST
Domaini1025 – 1222198B30.2/SPRY 2PROSITE-ProRule annotationAdd
BLAST
Domaini1337 – 1562226B30.2/SPRY 3PROSITE-ProRule annotationAdd
BLAST
Repeati2692 – 28101193Add
BLAST
Repeati2812 – 29251144Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni853 – 292520734 X approximate repeatsAdd
BLAST
Regioni3581 – 361030Interaction with CALMAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili4412 – 444534Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi4414 – 445542Glu-rich (acidic)Add
BLAST

Domaini

The calcium release channel activity resides in the C-terminal region while the remaining part of the protein resides in the cytoplasm.Curated

Sequence similaritiesi

Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR2 subfamily. [View classification]Curated
Contains 3 B30.2/SPRY domains.PROSITE-ProRule annotation
Contains 5 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG247670.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiQ92736.
KOiK04962.
OrthoDBiEOG71K622.
PhylomeDBiQ92736.
TreeFamiTF315244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
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.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 1 hit.
PfamiPF08709. 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]
PRINTSiPR00795. RYANODINER.
SMARTiSM00054. EFh. 2 hits.
SM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92736-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MADGGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE 
        60         70         80         90        100
STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF 
       110        120        130        140        150
MMKTAQGGGH RTLLYGHAIL LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ 
       160        170        180        190        200
EDTTGEACWW TIHPASKQRS EGEKVRVGDD LILVSVSSER YLHLSYGNGS 
       210        220        230        240        250
LHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH MDECLTVPSG 
       260        270        280        290        300
EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV 
       310        320        330        340        350
TTGKYLSLME DKNLLLMDKE KADVKSTAFT FRSSKEKLDV GVRKEVDGMG 
       360        370        380        390        400
TSEIKYGDSV CYIQHVDTGL WLTYQSVDVK SVRMGSIQRK AIMHHEGHMD 
       410        420        430        440        450
DGISLSRSQH EESRTARVIR STVFLFNRFI RGLDALSKKA KASTVDLPIE 
       460        470        480        490        500
SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR ALKNRQNLFQ EEGMINLVLE 
       510        520        530        540        550
CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL IRGNRKNCAQ 
       560        570        580        590        600
FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL 
       610        620        630        640        650
LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN 
       660        670        680        690        700
HVSSMRPNIF LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST 
       710        720        730        740        750
EGYSPYPGGG EEWGGNGVGD DLFSYGFDGL HLWSGCIART VSSPNQHLLR 
       760        770        780        790        800
TDDVISCCLD LSAPSISFRI NGQPVQGMFE NFNIDGLFFP VVSFSAGIKV 
       810        820        830        840        850
RFLLGGRHGE FKFLPPPGYA PCYEAVLPKE KLKVEHSREY KQERTYTRDL 
       860        870        880        890        900
LGPTVSLTQA AFTPIPVDTS QIVLPPHLER IREKLAENIH ELWVMNKIEL 
       910        920        930        940        950
GWQYGPVRDD NKRQHPCLVE FSKLPEQERN YNLQMSLETL KTLLALGCHV 
       960        970        980        990       1000
GISDEHAEDK VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA 
      1010       1020       1030       1040       1050
ENAHNVWARD RIRQGWTYGI QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL 
      1060       1070       1080       1090       1100
REAVRTLLGY GYNLEAPDQD HAARAEVCSG TGERFRIFRA EKTYAVKAGR 
      1110       1120       1130       1140       1150
WYFEFETVTA GDMRVGWSRP GCQPDQELGS DERAFAFDGF KAQRWHQGNE 
      1160       1170       1180       1190       1200
HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG 
      1210       1220       1230       1240       1250
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW 
      1260       1270       1280       1290       1300
LSKRLPQFLQ VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNSNTDIM 
      1310       1320       1330       1340       1350
FYRLSMPIEC AEVFSKTVAG GLPGAGLFGP KNDLEDYDAD SDFEVLMKTA 
      1360       1370       1380       1390       1400
HGHLVPDRVD KDKEATKPEF NNHKDYAQEK PSRLKQRFLL RRTKPDYSTS 
      1410       1420       1430       1440       1450
HSARLTEDVL ADDRDDYDFL MQTSTYYYSV RIFPGQEPAN VWVGWITSDF 
      1460       1470       1480       1490       1500
HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR 
      1510       1520       1530       1540       1550
NNNGLEIGCV VDAASGLLTF IANGKELSTY YQVEPSTKLF PAVFAQATSP 
      1560       1570       1580       1590       1600
NVFQFELGRI KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRMP 
      1610       1620       1630       1640       1650
NQFLKVDVSR ISERQGWLVQ CLDPLQFMSL HIPEENRSVD ILELTEQEEL 
      1660       1670       1680       1690       1700
LKFHYHTLRL YSAVCALGNH RVAHALCSHV DEPQLLYAIE NKYMPGLLRA 
      1710       1720       1730       1740       1750
GYYDLLIDIH LSSYATARLM MNNEYIVPMT EETKSITLFP DENKKHGLPG 
      1760       1770       1780       1790       1800
IGLSTSLRPR MQFSSPSFVS ISNECYQYSP EFPLDILKSK TIQMLTEAVK 
      1810       1820       1830       1840       1850
EGSLHARDPV GGTTEFLFVP LIKLFYTLLI MGIFHNEDLK HILQLIEPSV 
      1860       1870       1880       1890       1900
FKEAATPEEE SDTLEKELSV DDAKLQGAGE EEAKGGKRPK EGLLQMKLPE 
      1910       1920       1930       1940       1950
PVKLQMCLLL QYLCDCQVRH RIEAIVAFSD DFVAKLQDNQ RFRYNEVMQA 
      1960       1970       1980       1990       2000
LNMSAALTAR KTKEFRSPPQ EQINMLLNFK DDKSECPCPE EIRDQLLDFH 
      2010       2020       2030       2040       2050
EDLMTHCGIE LDEDGSLDGN SDLTIRGRLL SLVEKVTYLK KKQAEKPVES 
      2060       2070       2080       2090       2100
DSKKSSTLQQ LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR 
      2110       2120       2130       2140       2150
ALPKTYTING VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM 
      2160       2170       2180       2190       2200
NNKVFYQHPN LMRALGMHET VMEVMVNVLG GGESKEITFP KMVANCCRFL 
      2210       2220       2230       2240       2250
CYFCRISRQN QKAMFDHLSY LLENSSVGLA SPAMRGSTPL DVAAASVMDN 
      2260       2270       2280       2290       2300
NELALALREP DLEKVVRYLA GCGLQSCQML VSKGYPDIGW NPVEGERYLD 
      2310       2320       2330       2340       2350
FLRFAVFCNG ESVEENANVV VRLLIRRPEC FGPALRGEGG NGLLAAMEEA 
      2360       2370       2380       2390       2400
IKIAEDPSRD GPSPNSGSSK TLDTEEEEDD TIHMGNAIMT FYSALIDLLG 
      2410       2420       2430       2440       2450
RCAPEMHLIH AGKGEAIRIR SILRSLIPLG DLVGVISIAF QMPTIAKDGN 
      2460       2470       2480       2490       2500
VVEPDMSAGF CPDHKAAMVL FLDRVYGIEV QDFLLHLLEV GFLPDLRAAA 
      2510       2520       2530       2540       2550
SLDTAALSAT DMALALNRYL CTAVLPLLTR CAPLFAGTEH HASLIDSLLH 
      2560       2570       2580       2590       2600
TVYRLSKGCS LTKAQRDSIE VCLLSICGQL RPSMMQHLLR RLVFDVPLLN 
      2610       2620       2630       2640       2650
EHAKMPLKLL TNHYERCWKY YCLPGGWGNF GAASEEELHL SRKLFWGIFD 
      2660       2670       2680       2690       2700
ALSQKKYEQE LFKLALPCLS AVAGALPPDY MESNYVSMME KQSSMDSEGN 
      2710       2720       2730       2740       2750
FNPQPVDTSN ITIPEKLEYF INKYAEHSHD KWSMDKLANG WIYGEIYSDS 
      2760       2770       2780       2790       2800
SKVQPLMKPY KLLSEKEKEI YRWPIKESLK TMLAWGWRIE RTREGDSMAL 
      2810       2820       2830       2840       2850
YNRTRRISQT SQVSVDAAHG YSPRAIDMSN VTLSRDLHAM AEMMAENYHN 
      2860       2870       2880       2890       2900
IWAKKKKMEL ESKGGGNHPL LVPYDTLTAK EKAKDREKAQ DILKFLQING 
      2910       2920       2930       2940       2950
YAVSRGFKDL ELDTPSIEKR FAYSFLQQLI RYVDEAHQYI LEFDGGSRGK 
      2960       2970       2980       2990       3000
GEHFPYEQEI KFFAKVVLPL IDQYFKNHRL YFLSAASRPL CSGGHASNKE 
      3010       3020       3030       3040       3050
KEMVTSLFCK LGVLVRHRIS LFGNDATSIV NCLHILGQTL DARTVMKTGL 
      3060       3070       3080       3090       3100
ESVKSALRAF LDNAAEDLEK TMENLKQGQF THTRNQPKGV TQIINYTTVA 
      3110       3120       3130       3140       3150
LLPMLSSLFE HIGQHQFGED LILEDVQVSC YRILTSLYAL GTSKSIYVER 
      3160       3170       3180       3190       3200
QRSALGECLA AFAGAFPVAF LETHLDKHNI YSIYNTKSSR ERAALSLPTN 
      3210       3220       3230       3240       3250
VEDVCPNIPS LEKLMEEIVE LAESGIRYTQ MPHVMEVILP MLCSYMSRWW 
      3260       3270       3280       3290       3300
EHGPENNPER AEMCCTALNS EHMNTLLGNI LKIIYNNLGI DEGAWMKRLA 
      3310       3320       3330       3340       3350
VFSQPIINKV KPQLLKTHFL PLMEKLKKKA ATVVSEEDHL KAEARGDMSE 
      3360       3370       3380       3390       3400
AELLILDEFT TLARDLYAFY PLLIRFVDYN RAKWLKEPNP EAEELFRMVA 
      3410       3420       3430       3440       3450
EVFIYWSKSH NFKREEQNFV VQNEINNMSF LITDTKSKMS KAAVSDQERK 
      3460       3470       3480       3490       3500
KMKRKGDRYS MQTSLIVAAL KRLLPIGLNI CAPGDQELIA LAKNRFSLKD 
      3510       3520       3530       3540       3550
TEDEVRDIIR SNIHLQGKLE DPAIRWQMAL YKDLPNRTDD TSDPEKTVER 
      3560       3570       3580       3590       3600
VLDIANVLFH LEQKSKRVGR RHYCLVEHPQ RSKKAVWHKL LSKQRKRAVV 
      3610       3620       3630       3640       3650
ACFRMAPLYN LPRHRAVNLF LQGYEKSWIE TEEHYFEDKL IEDLAKPGAE 
      3660       3670       3680       3690       3700
PPEEDEGTKR VDPLHQLILL FSRTALTEKC KLEEDFLYMA YADIMAKSCH 
      3710       3720       3730       3740       3750
DEEDDDGEEE VKSFEEKEME KQKLLYQQAR LHDRGAAEMV LQTISASKGE 
      3760       3770       3780       3790       3800
TGPMVAATLK LGIAILNGGN STVQQKMLDY LKEKKDVGFF QSLAGLMQSC 
      3810       3820       3830       3840       3850
SVLDLNAFER QNKAEGLGMV TEEGSGEKVL QDDEFTCDLF RFLQLLCEGH 
      3860       3870       3880       3890       3900
NSDFQNYLRT QTGNNTTVNI IISTVDYLLR VQESISDFYW YYSGKDVIDE 
      3910       3920       3930       3940       3950
QGQRNFSKAI QVAKQVFNTL TEYIQGPCTG NQQSLAHSRL WDAVVGFLHV 
      3960       3970       3980       3990       4000
FAHMQMKLSQ DSSQIELLKE LMDLQKDMVV MLLSMLEGNV VNGTIGKQMV 
      4010       4020       4030       4040       4050
DMLVESSNNV EMILKFFDMF LKLKDLTSSD TFKEYDPDGK GVISKRDFHK 
      4060       4070       4080       4090       4100
AMESHKHYTQ SETEFLLSCA ETDENETLDY EEFVKRFHEP AKDIGFNVAV 
      4110       4120       4130       4140       4150
LLTNLSEHMP NDTRLQTFLE LAESVLNYFQ PFLGRIEIMG SAKRIERVYF 
      4160       4170       4180       4190       4200
EISESSRTQW EKPQVKESKR QFIFDVVNEG GEKEKMELFV NFCEDTIFEM 
      4210       4220       4230       4240       4250
QLAAQISESD LNERSANKEE SEKERPEEQG PRMAFFSILT VRSALFALRY 
      4260       4270       4280       4290       4300
NILTLMRMLS LKSLKKQMKK VKKMTVKDMV TAFFSSYWSI FMTLLHFVAS 
      4310       4320       4330       4340       4350
VFRGFFRIIC SLLLGGSLVE GAKKIKVAEL LANMPDPTQD EVRGDGEEGE 
      4360       4370       4380       4390       4400
RKPLEAALPS EDLTDLKELT EESDLLSDIF GLDLKREGGQ YKLIPHNPNA 
      4410       4420       4430       4440       4450
GLSDLMSNPV PMPEVQEKFQ EQKAKEEEKE EKEETKSEPE KAEGEDGEKE 
      4460       4470       4480       4490       4500
EKAKEDKGKQ KLRQLHTHRY GEPEVPESAF WKKIIAYQQK LLNYFARNFY 
      4510       4520       4530       4540       4550
NMRMLALFVA FAINFILLFY KVSTSSVVEG KELPTRSSSE NAKVTSLDSS 
      4560       4570       4580       4590       4600
SHRIIAVHYV LEESSGYMEP TLRILAILHT VISFFCIIGY YCLKVPLVIF 
      4610       4620       4630       4640       4650
KREKEVARKL EFDGLYITEQ PSEDDIKGQW DRLVINTQSF PNNYWDKFVK 
      4660       4670       4680       4690       4700
RKVMDKYGEF YGRDRISELL GMDKAALDFS DAREKKKPKK DSSLSAVLNS 
      4710       4720       4730       4740       4750
IDVKYQMWKL GVVFTDNSFL YLAWYMTMSV LGHYNNFFFA AHLLDIAMGF 
      4760       4770       4780       4790       4800
KTLRTILSSV THNGKQLVLT VGLLAVVVYL YTVVAFNFFR KFYNKSEDGD 
      4810       4820       4830       4840       4850
TPDMKCDDML TCYMFHMYVG VRAGGGIGDE IEDPAGDEYE IYRIIFDITF 
      4860       4870       4880       4890       4900
FFFVIVILLA IIQGLIIDAF GELRDQQEQV KEDMETKCFI CGIGNDYFDT 
      4910       4920       4930       4940       4950
VPHGFETHTL QEHNLANYLF FLMYLINKDE TEHTGQESYV WKMYQERCWE 
      4960 
FFPAGDCFRK QYEDQLN
Length:4,967
Mass (Da):564,567
Last modified:October 5, 2010 - v3
Checksum:i44984485F8677B42
GO
Isoform 2 (identifier: Q92736-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3715-3715: E → EVTGSQRSK

Show »
Length:4,975
Mass (Da):565,411
Checksum:iC24909FF9BC665B6
GO

Sequence cautioni

The sequence CAH71369.1 differs from that shown.Erroneous gene model prediction.Curated
The sequence CAH71393.1 differs from that shown.Erroneous gene model prediction.Curated
The sequence CAH73918.1 differs from that shown.Erroneous gene model prediction.Curated
The sequence CAI14440.1 differs from that shown.Erroneous gene model prediction.Curated
The sequence CAI15350.1 differs from that shown.Erroneous gene model prediction.Curated
The sequence CAI15936.1 differs from that shown.Erroneous gene model prediction.Curated
The sequence CAI22065.1 differs from that shown.Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1037 – 10371L → P in CAA66975. (PubMed:8809036)Curated
Sequence conflicti1037 – 10371L → P in CAC18855. (PubMed:11159936)Curated
Sequence conflicti2785 – 27895WGWRI → RTMRT in CAA66975. (PubMed:8809036)Curated
Sequence conflicti2785 – 27895WGWRI → RTMRT in CAC18855. (PubMed:11159936)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti164 – 1641P → S in CPVT1. 1 Publication
VAR_044086
Natural varianti176 – 1761R → Q in ARVD2 and CPVT1. 2 Publications
VAR_044087
Natural varianti414 – 4141R → L in CPVT1. 1 Publication
VAR_044088
Natural varianti419 – 4191I → F in CPVT1. 1 Publication
VAR_044089
Natural varianti420 – 4201R → W in CPVT1. 2 Publications
Corresponds to variant rs190140598 [ dbSNP | Ensembl ].		VAR_044090
Natural varianti433 – 4331L → P in ARVD2 and CPVT1. 2 Publications
VAR_011395
Natural varianti507 – 5071V → I.
Corresponds to variant rs16835270 [ dbSNP | Ensembl ].		VAR_044091
Natural varianti1886 – 18861G → S.
Corresponds to variant rs3766871 [ dbSNP | Ensembl ].		VAR_022078
Natural varianti2246 – 22461S → L in CPVT1. 3 Publications
VAR_011396
Natural varianti2306 – 23061V → I in CPVT1. 1 Publication
VAR_023694
Natural varianti2311 – 23111E → D in CPVT1. 1 Publication
VAR_044092
Natural varianti2328 – 23281P → S in CPVT1. 1 Publication
VAR_011397
Natural varianti2386 – 23861N → I in ARVD2 and CPVT1. 2 Publications
VAR_011398
Natural varianti2387 – 23871A → P in CPVT1. 1 Publication
VAR_044093
Natural varianti2392 – 23921Y → C in CPVT1. 1 Publication
VAR_044094
Natural varianti2403 – 24031A → T in CPVT1. 1 Publication
VAR_044095
Natural varianti2474 – 24741R → S in CPVT1. 2 Publications
VAR_011399
Natural varianti2504 – 25041T → M in ARVD2 and CPVT1. 2 Publications
VAR_044096
Natural varianti2958 – 29581Q → R.1 Publication
Corresponds to variant rs34967813 [ dbSNP | Ensembl ].		VAR_011590
Natural varianti3778 – 37781L → F in CPVT1. 1 Publication
VAR_044097
Natural varianti3946 – 39461G → S in CPVT1. 1 Publication
VAR_044098
Natural varianti4097 – 40971N → S in CPVT1. 1 Publication
VAR_044099
Natural varianti4104 – 41041N → K in CPVT1. 2 Publications
VAR_011400
Natural varianti4146 – 41461E → K in CPVT1. 1 Publication
VAR_044100
Natural varianti4158 – 41581T → P in CPVT1. 1 Publication
VAR_044101
Natural varianti4201 – 42011Q → R in CPVT1. 1 Publication
VAR_011401
Natural varianti4497 – 44971R → C in CPVT1. 3 Publications
VAR_011402
Natural varianti4499 – 44991F → C in CPVT1. 1 Publication
VAR_044102
Natural varianti4504 – 45041M → I in CPVT1. 1 Publication
VAR_044103
Natural varianti4510 – 45101A → T in CPVT1. 1 Publication
VAR_044104
Natural varianti4607 – 46071A → P in CPVT1. 1 Publication
VAR_044105
Natural varianti4653 – 46531V → F in CPVT1. 1 Publication
VAR_011403
Natural varianti4671 – 46711G → R in CPVT1. 1 Publication
VAR_044106
Natural varianti4771 – 47711V → I in CPVT1. 1 Publication
VAR_044107
Natural varianti4848 – 48481I → V in CPVT1. 1 Publication
VAR_044108
Natural varianti4860 – 48601A → G in CPVT1; diminishes the response to activation by luminal Ca(2+) but has little effect on the sensitivity of the channel to activation by cytosolic Ca(2+); shows caffeine-induced Ca(2+) release but exhibits no store-overload-induced Ca(2+) release (SOICR); HL1 cardiac cells transfected with the G-4860 mutant displayed attenuated SOICR activity compared to cells transfected with wild-type RYR2. 2 Publications
VAR_044109
Natural varianti4867 – 48671I → M in CPVT1. 1 Publication
VAR_044110
Natural varianti4880 – 48801V → A in CPVT1. 1 Publication
VAR_044111
Natural varianti4895 – 48951N → D in CPVT1. 1 Publication
VAR_044112
Natural varianti4902 – 49021P → L in CPVT1. 1 Publication
VAR_023695
Natural varianti4950 – 49501E → K in CPVT1. 1 Publication
VAR_044113
Natural varianti4959 – 49591R → Q in CPVT1. 1 Publication
VAR_023696

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3715 – 37151E → EVTGSQRSK in isoform 2. CuratedVSP_005953

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98330 mRNA. Translation: CAA66975.1.
AJ300340
, AJ300341, AJ300342, AJ300343, AJ300347, AJ300349, AJ300351, AJ300353, AJ300355, AJ300364, AJ300363, AJ300362, AJ300361, AJ300360, AJ300359, AJ300358, AJ300357, AJ300356, AJ300373, AJ300372, AJ300371, AJ300370, AJ300369, AJ300368, AJ300367, AJ300366, AJ300365, AJ300382, AJ300381, AJ300380, AJ300379, AJ300378, AJ300377, AJ300376, AJ300375, AJ300374, AJ300399, AJ300398, AJ300397, AJ300396, AJ300395, AJ300394, AJ300393, AJ300392, AJ300391, AJ300416, AJ300415, AJ300414, AJ300413, AJ300412, AJ300411, AJ300410, AJ300409, AJ300408, AJ300433, AJ300432, AJ300431, AJ300430, AJ300429, AJ300428, AJ300427, AJ300426, AJ300425, AJ300444, AJ300443, AJ300442, AJ300441, AJ300440, AJ300439, AJ300438, AJ300437, AJ300436, AJ300435, AJ300434, AJ300424, AJ300423, AJ300422, AJ300421, AJ300420, AJ300419, AJ300418, AJ300417, AJ300407, AJ300406, AJ300405, AJ300404, AJ300403, AJ300402, AJ300401, AJ300400, AJ300390, AJ300389, AJ300388, AJ300387, AJ300386, AJ300385, AJ300384, AJ300383, AJ300354, AJ300352, AJ300350, AJ300348, AJ300346, AJ300345, AJ300344 Genomic DNA. Translation: CAC18855.1.
AL365332
, AL356773, AL359924, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAH71369.1. Sequence problems.
AL445473
, AL356773, AL359924, AL365332, AL391809, AL442065, AL513130 Genomic DNA. Translation: CAH71393.1. Sequence problems.
AL356773
, AL359924, AL365332, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAH73918.1. Sequence problems.
AL391809
, AL356773, AL359924, AL365332, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAI14440.1. Sequence problems.
AL442065
, AL356773, AL359924, AL365332, AL391809, AL445473, AL513130 Genomic DNA. Translation: CAI15350.1. Sequence problems.
AL513130
, AL356773, AL359924, AL365332, AL391809, AL442065, AL445473 Genomic DNA. Translation: CAI15936.1. Sequence problems.
AL359924
, AL356773, AL365332, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAI22065.1. Sequence problems.
Y08218 mRNA. Translation: CAA69395.1.
X91869 mRNA. Translation: CAA62975.1.
AJ002511 mRNA. Translation: CAA05502.1.
CCDSiCCDS55691.1. [Q92736-1]
PIRiS72269.
RefSeqiNP_001026.2. NM_001035.2. [Q92736-1]
XP_006711868.1. XM_006711805.1. [Q92736-2]
UniGeneiHs.109514.
Hs.738571.

Genome annotation databases

EnsembliENST00000366574; ENSP00000355533; ENSG00000198626. [Q92736-1]
GeneIDi6262.
KEGGihsa:6262.
UCSCiuc001hyl.1. human. [Q92736-1]

Polymorphism databases

DMDMi308153558.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ryanodine receptor entry

Wikipedia

RYR2 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98330 mRNA. Translation: CAA66975.1.
AJ300340
, AJ300341, AJ300342, AJ300343, AJ300347, AJ300349, AJ300351, AJ300353, AJ300355, AJ300364, AJ300363, AJ300362, AJ300361, AJ300360, AJ300359, AJ300358, AJ300357, AJ300356, AJ300373, AJ300372, AJ300371, AJ300370, AJ300369, AJ300368, AJ300367, AJ300366, AJ300365, AJ300382, AJ300381, AJ300380, AJ300379, AJ300378, AJ300377, AJ300376, AJ300375, AJ300374, AJ300399, AJ300398, AJ300397, AJ300396, AJ300395, AJ300394, AJ300393, AJ300392, AJ300391, AJ300416, AJ300415, AJ300414, AJ300413, AJ300412, AJ300411, AJ300410, AJ300409, AJ300408, AJ300433, AJ300432, AJ300431, AJ300430, AJ300429, AJ300428, AJ300427, AJ300426, AJ300425, AJ300444, AJ300443, AJ300442, AJ300441, AJ300440, AJ300439, AJ300438, AJ300437, AJ300436, AJ300435, AJ300434, AJ300424, AJ300423, AJ300422, AJ300421, AJ300420, AJ300419, AJ300418, AJ300417, AJ300407, AJ300406, AJ300405, AJ300404, AJ300403, AJ300402, AJ300401, AJ300400, AJ300390, AJ300389, AJ300388, AJ300387, AJ300386, AJ300385, AJ300384, AJ300383, AJ300354, AJ300352, AJ300350, AJ300348, AJ300346, AJ300345, AJ300344 Genomic DNA. Translation: CAC18855.1.
AL365332
, AL356773, AL359924, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAH71369.1. Sequence problems.
AL445473
, AL356773, AL359924, AL365332, AL391809, AL442065, AL513130 Genomic DNA. Translation: CAH71393.1. Sequence problems.
AL356773
, AL359924, AL365332, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAH73918.1. Sequence problems.
AL391809
, AL356773, AL359924, AL365332, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAI14440.1. Sequence problems.
AL442065
, AL356773, AL359924, AL365332, AL391809, AL445473, AL513130 Genomic DNA. Translation: CAI15350.1. Sequence problems.
AL513130
, AL356773, AL359924, AL365332, AL391809, AL442065, AL445473 Genomic DNA. Translation: CAI15936.1. Sequence problems.
AL359924
, AL356773, AL365332, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAI22065.1. Sequence problems.
Y08218 mRNA. Translation: CAA69395.1.
X91869 mRNA. Translation: CAA62975.1.
AJ002511 mRNA. Translation: CAA05502.1.
CCDSiCCDS55691.1. [Q92736-1]
PIRiS72269.
RefSeqiNP_001026.2. NM_001035.2. [Q92736-1]
XP_006711868.1. XM_006711805.1. [Q92736-2]
UniGeneiHs.109514.
Hs.738571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JKQX-ray2.39A1-606[»]
ProteinModelPortaliQ92736.
SMRiQ92736. Positions 10-544, 862-1068, 1082-1218, 2701-2905, 3581-3607, 4030-4086.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112174. 25 interactions.
DIPiDIP-38325N.
IntActiQ92736. 9 interactions.
MINTiMINT-1201008.
STRINGi9606.ENSP00000355533.

Chemistry

GuidetoPHARMACOLOGYi748.

Protein family/group databases

TCDBi1.A.3.1.1. the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.

PTM databases

PhosphoSiteiQ92736.

Polymorphism databases

DMDMi308153558.

Proteomic databases

MaxQBiQ92736.
PaxDbiQ92736.
PRIDEiQ92736.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366574; ENSP00000355533; ENSG00000198626. [Q92736-1]
GeneIDi6262.
KEGGihsa:6262.
UCSCiuc001hyl.1. human. [Q92736-1]

Organism-specific databases

CTDi6262.
GeneCardsiGC01P237205.
GeneReviewsiRYR2.
HGNCiHGNC:10484. RYR2.
HPAiCAB006834.
HPA016697.
HPA020028.
MIMi180902. gene.
600996. phenotype.
604772. phenotype.
neXtProtiNX_Q92736.
Orphaneti3286. Catecholaminergic polymorphic ventricular tachycardia.
293899. Familial isolated arrhythmogenic ventricular dysplasia, biventricular form.
293888. Familial isolated arrhythmogenic ventricular dysplasia, left dominant form.
293910. Familial isolated arrhythmogenic ventricular dysplasia, right dominant form.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG247670.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiQ92736.
KOiK04962.
OrthoDBiEOG71K622.
PhylomeDBiQ92736.
TreeFamiTF315244.

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.

Miscellaneous databases

ChiTaRSiRYR2. human.
GeneWikiiRyanodine_receptor_2.
GenomeRNAii6262.
NextBioi24325.
PROiQ92736.
SOURCEiSearch...

Gene expression databases

BgeeiQ92736.
CleanExiHS_RYR2.
ExpressionAtlasiQ92736. baseline and differential.
GenevestigatoriQ92736.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
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.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 1 hit.
PfamiPF08709. 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]
PRINTSiPR00795. RYANODINER.
SMARTiSM00054. EFh. 2 hits.
SM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human cardiac muscle ryanodine receptor-calcium release channel: identification, primary structure and topological analysis."
    Tunwell R.E.A., Wickenden C., Bertrand B.M.A., Shevchenko V.I., Walsh M.B., Allen P.D., Lai F.A.
    Biochem. J. 318:477-487(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Heart muscle.
  2. "Identification of mutations in the cardiac ryanodine receptor gene in families affected with arrhythmogenic right ventricular cardiomyopathy type 2 (ARVD2)."
    Tiso N., Stephan D.A., Nava A., Bagattin A., Devaney J.M., Stanchi F., Larderet G., Brahmbhatt B., Brown K., Bauce B., Muriago M., Basso C., Thiene G., Danieli G.A., Rampazzo A.
    Hum. Mol. Genet. 10:189-194(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARVD2 GLN-176; PRO-433; ILE-2386 AND MET-2504.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Differential expression of ryanodine receptor RyR2 mRNA in the non-pregnant and pregnant human myometrium."
    Awad S.S., Lamb H.K., Morgan J.M., Dunlop W., Gillespie J.I.
    Biochem. J. 322:777-783(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-87 AND 533-681, DEVELOPMENTAL STAGE, INDUCTION BY TGFB1.
    Tissue: Heart muscle and Myometrium.
  5. "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: NUCLEOTIDE SEQUENCE [MRNA] OF 4292-4479, TISSUE SPECIFICITY.
    Tissue: Cerebellum and Hippocampus.
  6. "PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts."
    Marx S.O., Reiken S., Hisamatsu Y., Jayaraman T., Burkhoff D., Rosemblit N., Marks A.R.
    Cell 101:365-376(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH FKBP1B; PP1; PP2A AKAP6 AND PKA, INTERACTION WITH FKBP1B; PKA; PP1 AND PP2A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-2808, PHOSPHORYLATION AT SER-2808.
  7. "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.
  8. "CaMKII-dependent diastolic SR Ca2+ leak and elevated diastolic Ca2+ levels in right atrial myocardium of patients with atrial fibrillation."
    Neef S., Dybkova N., Sossalla S., Ort K.R., Fluschnik N., Neumann K., Seipelt R., Schondube F.A., Hasenfuss G., Maier L.S.
    Circ. Res. 106:1134-1144(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-2808 AND SER-2814.
  9. "Cardiac excitation-contraction coupling."
    Bers D.M.
    Nature 415:198-205(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  10. "Cardiac ryanodine receptor phosphorylation by CaM Kinase II: keeping the balance right."
    Currie S.
    Front. Biosci. 14:5134-5156(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  11. "Modulation of ryanodine receptor Ca2+ channels."
    Ozawa T.
    Mol. Med. Report. 3:199-204(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  12. "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.
  13. "Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia."
    Priori S.G., Napolitano C., Tiso N., Memmi M., Vignati G., Bloise R., Sorrentino V.V., Danieli G.A.
    Circulation 103:196-200(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VTSIP LEU-2246; SER-2474; LYS-4104 AND CYS-4497.
  14. "Mutations of the cardiac ryanodine receptor (RyR2) gene in familial polymorphic ventricular tachycardia."
    Laitinen P.J., Brown K.M., Piippo K., Swan H., Devaney J.M., Brahmbhatt B., Donarum E.A., Marino M., Tiso N., Viitasalo M., Toivonen L., Stephan D.A., Kontula K.
    Circulation 103:485-490(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CPVT1 SER-2328; ARG-4201 AND PHE-4653, VARIANT ARG-2958.
  15. "Clinical and molecular characterization of patients with catecholaminergic polymorphic ventricular tachycardia."
    Priori S.G., Napolitano C., Memmi M., Colombi B., Drago F., Gasparini M., DeSimone L., Coltorti F., Bloise R., Keegan R., Cruz Filho F.E.S., Vignati G., Benatar A., DeLogu A.
    Circulation 106:69-74(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CPVT1 LEU-2246; ASP-2311; SER-2474; PHE-3778; SER-3946; SER-3946; LYS-4104; CYS-4497; ILE-4771; GLY-4860; MET-4867; ASP-4895 AND LYS-4950.
  16. "Screening for ryanodine receptor type 2 mutations in families with effort-induced polymorphic ventricular arrhythmias and sudden death: early diagnosis of asymptomatic carriers."
    Bauce B., Rampazzo A., Basso C., Bagattin A., Daliento L., Tiso N., Turrini P., Thiene G., Danieli G.A., Nava A.
    J. Am. Coll. Cardiol. 40:341-349(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CPVT1 GLN-176; TRP-420; PRO-433; ILE-2386; CYS-2392 AND MET-2504.
  17. "Molecular genetics of exercise-induced polymorphic ventricular tachycardia: identification of three novel cardiac ryanodine receptor mutations and two common calsequestrin 2 amino-acid polymorphisms."
    Laitinen P.J., Swan H., Kontula K.
    Eur. J. Hum. Genet. 11:888-891(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VTSIP ILE-2306; LEU-4902 AND GLN-4959.
  18. "Spectrum and frequency of cardiac channel defects in swimming-triggered arrhythmia syndromes."
    Choi G., Kopplin L.J., Tester D.J., Will M.L., Haglund C.M., Ackerman M.J.
    Circulation 110:2119-2124(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CPVT1 SER-164; LEU-414; PHE-419; THR-2403; CYS-4499; THR-4510; ARG-4671 AND VAL-4848.
  19. "Gene symbol: RYR2. Disease: effort-induced polymorphic ventricular arrhythmias."
    Bagattin A., Veronese C., Rampazzo A., Danieli G.A.
    Hum. Genet. 114:404-404(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CPVT1 ILE-4504 AND ALA-4880.
  20. "Gene symbol: RYR2. Disease: effort-induced polymorphic ventricular arrhythmias."
    Bagattin A., Veronese C., Rampazzo A., Danieli G.A.
    Hum. Genet. 114:405-405(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CPVT1 PRO-2387 AND PRO-4607.
  21. "Targeted mutational analysis of the RyR2-encoded cardiac ryanodine receptor in sudden unexplained death: a molecular autopsy of 49 medical examiner/coroner's cases."
    Tester D.J., Spoon D.B., Valdivia H.H., Makielski J.C., Ackerman M.J.
    Mayo Clin. Proc. 79:1380-1384(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CPVT1 TRP-420; LEU-2246; SER-4097; LYS-4146; PRO-4158 AND CYS-4497.
  22. "Loss of luminal Ca(2+) activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden death."
    Jiang D., Chen W., Wang R., Zhang L., Chen S.R.W.
    Proc. Natl. Acad. Sci. U.S.A. 104:18309-18314(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT CPVT1 GLY-4860.
+Additional computationally mapped references.

Entry informationi

Entry nameiRYR2_HUMAN
AccessioniPrimary (citable) accession number: Q92736
Secondary accession number(s): Q15411, Q546N8, Q5T3P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 5, 2010
Last modified: February 4, 2015
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.