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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: 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 binding Source: UniProtKB
  11. protein kinase A catalytic subunit binding Source: BHF-UCL
  12. protein kinase A regulatory subunit binding Source: BHF-UCL
  13. ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  14. 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. Purkinje myocyte to ventricular cardiac muscle cell signaling Source: BHF-UCL
  24. regulation of cardiac muscle contraction Source: BHF-UCL
  25. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  26. regulation of heart rate Source: BHF-UCL
  27. release of sequestered calcium ion into cytosol Source: BHF-UCL
  28. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
  29. response to caffeine Source: BHF-UCL
  30. response to hypoxia Source: BHF-UCL
  31. response to redox state Source: BHF-UCL
  32. sarcoplasmic reticulum calcium ion transport Source: BHF-UCL
  33. transmembrane transport Source: Reactome
  34. type B pancreatic cell apoptotic process Source: BHF-UCL
  35. 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10484. RYR2.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 42814281Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei4282 – 430221Helical; Reviewed predictionAdd
BLAST
Transmembranei4504 – 452421Helical; Reviewed predictionAdd
BLAST
Transmembranei4580 – 460021Helical; Reviewed predictionAdd
BLAST
Transmembranei4730 – 475021Helical; Reviewed predictionAdd
BLAST
Transmembranei4769 – 478921Helical; Reviewed predictionAdd
BLAST
Intramembranei4820 – 482910Pore-forming; By similarity
Transmembranei4850 – 487021Helical; Reviewed predictionAdd
BLAST
Topological domaini4871 – 496797Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. calcium channel complex Source: BHF-UCL
  2. extracellular vesicular exosome Source: UniProt
  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. Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Arrhythmogenic right ventricular dysplasia, familial, 2 (ARVD2) [MIM:600996]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 cardiomyopathy (CPVT1) [MIM:604772]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.8 Publications
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 PKA By 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.
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

ArrayExpressiQ92736.
BgeeiQ92736.
CleanExiHS_RYR2.
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.2 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 – 2810
Beta strandi31 – 388
Beta strandi48 – 514
Turni53 – 575
Helixi63 – 653
Beta strandi67 – 737
Turni108 – 1103
Beta strandi118 – 12710
Beta strandi129 – 1324
Turni139 – 1413
Beta strandi145 – 1517
Beta strandi159 – 1668
Beta strandi180 – 1856
Turni186 – 1883
Beta strandi191 – 1966
Beta strandi198 – 20811
Beta strandi212 – 2187
Beta strandi233 – 2386
Turni239 – 2424
Beta strandi243 – 2464
Beta strandi250 – 2523
Helixi256 – 2583
Beta strandi261 – 2633
Helixi265 – 2695
Helixi271 – 2733
Beta strandi275 – 2806
Turni283 – 2864
Beta strandi295 – 2995
Turni300 – 3023
Beta strandi305 – 3084
Beta strandi310 – 3123
Beta strandi314 – 3174
Helixi319 – 3213
Helixi324 – 3274
Beta strandi329 – 3368
Beta strandi340 – 3423
Turni356 – 3583
Beta strandi360 – 3656
Turni366 – 3683
Beta strandi371 – 3755
Beta strandi388 – 3969
Beta strandi403 – 4075
Helixi410 – 43728
Helixi442 – 4443
Helixi449 – 46214
Helixi472 – 49120
Helixi494 – 50613
Beta strandi508 – 5103
Helixi511 – 5188
Helixi520 – 54122

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 16556MIR 1Add
BLAST
Domaini172 – 21746MIR 2Add
BLAST
Domaini225 – 28056MIR 3Add
BLAST
Domaini286 – 34358MIR 4Add
BLAST
Domaini351 – 40858MIR 5Add
BLAST
Domaini599 – 809211B30.2/SPRY 1Add
BLAST
Repeati853 – 9661141Add
BLAST
Repeati967 – 10801142Add
BLAST
Domaini1025 – 1222198B30.2/SPRY 2Add
BLAST
Domaini1337 – 1562226B30.2/SPRY 3Add
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 – 444534 Reviewed predictionAdd
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 Inferred.

Sequence similaritiesi

Contains 3 B30.2/SPRY domains.
Contains 5 MIR domains.

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG247670.
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.
IPR008985. ConA-like_lec_gl_sf.
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.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[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.

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MADGGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE     50
STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF 100
MMKTAQGGGH RTLLYGHAIL LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ 150
EDTTGEACWW TIHPASKQRS EGEKVRVGDD LILVSVSSER YLHLSYGNGS 200
LHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH MDECLTVPSG 250
EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV 300
TTGKYLSLME DKNLLLMDKE KADVKSTAFT FRSSKEKLDV GVRKEVDGMG 350
TSEIKYGDSV CYIQHVDTGL WLTYQSVDVK SVRMGSIQRK AIMHHEGHMD 400
DGISLSRSQH EESRTARVIR STVFLFNRFI RGLDALSKKA KASTVDLPIE 450
SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR ALKNRQNLFQ EEGMINLVLE 500
CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL IRGNRKNCAQ 550
FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL 600
LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN 650
HVSSMRPNIF LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST 700
EGYSPYPGGG EEWGGNGVGD DLFSYGFDGL HLWSGCIART VSSPNQHLLR 750
TDDVISCCLD LSAPSISFRI NGQPVQGMFE NFNIDGLFFP VVSFSAGIKV 800
RFLLGGRHGE FKFLPPPGYA PCYEAVLPKE KLKVEHSREY KQERTYTRDL 850
LGPTVSLTQA AFTPIPVDTS QIVLPPHLER IREKLAENIH ELWVMNKIEL 900
GWQYGPVRDD NKRQHPCLVE FSKLPEQERN YNLQMSLETL KTLLALGCHV 950
GISDEHAEDK VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA 1000
ENAHNVWARD RIRQGWTYGI QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL 1050
REAVRTLLGY GYNLEAPDQD HAARAEVCSG TGERFRIFRA EKTYAVKAGR 1100
WYFEFETVTA GDMRVGWSRP GCQPDQELGS DERAFAFDGF KAQRWHQGNE 1150
HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG 1200
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW 1250
LSKRLPQFLQ VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNSNTDIM 1300
FYRLSMPIEC AEVFSKTVAG GLPGAGLFGP KNDLEDYDAD SDFEVLMKTA 1350
HGHLVPDRVD KDKEATKPEF NNHKDYAQEK PSRLKQRFLL RRTKPDYSTS 1400
HSARLTEDVL ADDRDDYDFL MQTSTYYYSV RIFPGQEPAN VWVGWITSDF 1450
HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR 1500
NNNGLEIGCV VDAASGLLTF IANGKELSTY YQVEPSTKLF PAVFAQATSP 1550
NVFQFELGRI KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRMP 1600
NQFLKVDVSR ISERQGWLVQ CLDPLQFMSL HIPEENRSVD ILELTEQEEL 1650
LKFHYHTLRL YSAVCALGNH RVAHALCSHV DEPQLLYAIE NKYMPGLLRA 1700
GYYDLLIDIH LSSYATARLM MNNEYIVPMT EETKSITLFP DENKKHGLPG 1750
IGLSTSLRPR MQFSSPSFVS ISNECYQYSP EFPLDILKSK TIQMLTEAVK 1800
EGSLHARDPV GGTTEFLFVP LIKLFYTLLI MGIFHNEDLK HILQLIEPSV 1850
FKEAATPEEE SDTLEKELSV DDAKLQGAGE EEAKGGKRPK EGLLQMKLPE 1900
PVKLQMCLLL QYLCDCQVRH RIEAIVAFSD DFVAKLQDNQ RFRYNEVMQA 1950
LNMSAALTAR KTKEFRSPPQ EQINMLLNFK DDKSECPCPE EIRDQLLDFH 2000
EDLMTHCGIE LDEDGSLDGN SDLTIRGRLL SLVEKVTYLK KKQAEKPVES 2050
DSKKSSTLQQ LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR 2100
ALPKTYTING VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM 2150
NNKVFYQHPN LMRALGMHET VMEVMVNVLG GGESKEITFP KMVANCCRFL 2200
CYFCRISRQN QKAMFDHLSY LLENSSVGLA SPAMRGSTPL DVAAASVMDN 2250
NELALALREP DLEKVVRYLA GCGLQSCQML VSKGYPDIGW NPVEGERYLD 2300
FLRFAVFCNG ESVEENANVV VRLLIRRPEC FGPALRGEGG NGLLAAMEEA 2350
IKIAEDPSRD GPSPNSGSSK TLDTEEEEDD TIHMGNAIMT FYSALIDLLG 2400
RCAPEMHLIH AGKGEAIRIR SILRSLIPLG DLVGVISIAF QMPTIAKDGN 2450
VVEPDMSAGF CPDHKAAMVL FLDRVYGIEV QDFLLHLLEV GFLPDLRAAA 2500
SLDTAALSAT DMALALNRYL CTAVLPLLTR CAPLFAGTEH HASLIDSLLH 2550
TVYRLSKGCS LTKAQRDSIE VCLLSICGQL RPSMMQHLLR RLVFDVPLLN 2600
EHAKMPLKLL TNHYERCWKY YCLPGGWGNF GAASEEELHL SRKLFWGIFD 2650
ALSQKKYEQE LFKLALPCLS AVAGALPPDY MESNYVSMME KQSSMDSEGN 2700
FNPQPVDTSN ITIPEKLEYF INKYAEHSHD KWSMDKLANG WIYGEIYSDS 2750
SKVQPLMKPY KLLSEKEKEI YRWPIKESLK TMLAWGWRIE RTREGDSMAL 2800
YNRTRRISQT SQVSVDAAHG YSPRAIDMSN VTLSRDLHAM AEMMAENYHN 2850
IWAKKKKMEL ESKGGGNHPL LVPYDTLTAK EKAKDREKAQ DILKFLQING 2900
YAVSRGFKDL ELDTPSIEKR FAYSFLQQLI RYVDEAHQYI LEFDGGSRGK 2950
GEHFPYEQEI KFFAKVVLPL IDQYFKNHRL YFLSAASRPL CSGGHASNKE 3000
KEMVTSLFCK LGVLVRHRIS LFGNDATSIV NCLHILGQTL DARTVMKTGL 3050
ESVKSALRAF LDNAAEDLEK TMENLKQGQF THTRNQPKGV TQIINYTTVA 3100
LLPMLSSLFE HIGQHQFGED LILEDVQVSC YRILTSLYAL GTSKSIYVER 3150
QRSALGECLA AFAGAFPVAF LETHLDKHNI YSIYNTKSSR ERAALSLPTN 3200
VEDVCPNIPS LEKLMEEIVE LAESGIRYTQ MPHVMEVILP MLCSYMSRWW 3250
EHGPENNPER AEMCCTALNS EHMNTLLGNI LKIIYNNLGI DEGAWMKRLA 3300
VFSQPIINKV KPQLLKTHFL PLMEKLKKKA ATVVSEEDHL KAEARGDMSE 3350
AELLILDEFT TLARDLYAFY PLLIRFVDYN RAKWLKEPNP EAEELFRMVA 3400
EVFIYWSKSH NFKREEQNFV VQNEINNMSF LITDTKSKMS KAAVSDQERK 3450
KMKRKGDRYS MQTSLIVAAL KRLLPIGLNI CAPGDQELIA LAKNRFSLKD 3500
TEDEVRDIIR SNIHLQGKLE DPAIRWQMAL YKDLPNRTDD TSDPEKTVER 3550
VLDIANVLFH LEQKSKRVGR RHYCLVEHPQ RSKKAVWHKL LSKQRKRAVV 3600
ACFRMAPLYN LPRHRAVNLF LQGYEKSWIE TEEHYFEDKL IEDLAKPGAE 3650
PPEEDEGTKR VDPLHQLILL FSRTALTEKC KLEEDFLYMA YADIMAKSCH 3700
DEEDDDGEEE VKSFEEKEME KQKLLYQQAR LHDRGAAEMV LQTISASKGE 3750
TGPMVAATLK LGIAILNGGN STVQQKMLDY LKEKKDVGFF QSLAGLMQSC 3800
SVLDLNAFER QNKAEGLGMV TEEGSGEKVL QDDEFTCDLF RFLQLLCEGH 3850
NSDFQNYLRT QTGNNTTVNI IISTVDYLLR VQESISDFYW YYSGKDVIDE 3900
QGQRNFSKAI QVAKQVFNTL TEYIQGPCTG NQQSLAHSRL WDAVVGFLHV 3950
FAHMQMKLSQ DSSQIELLKE LMDLQKDMVV MLLSMLEGNV VNGTIGKQMV 4000
DMLVESSNNV EMILKFFDMF LKLKDLTSSD TFKEYDPDGK GVISKRDFHK 4050
AMESHKHYTQ SETEFLLSCA ETDENETLDY EEFVKRFHEP AKDIGFNVAV 4100
LLTNLSEHMP NDTRLQTFLE LAESVLNYFQ PFLGRIEIMG SAKRIERVYF 4150
EISESSRTQW EKPQVKESKR QFIFDVVNEG GEKEKMELFV NFCEDTIFEM 4200
QLAAQISESD LNERSANKEE SEKERPEEQG PRMAFFSILT VRSALFALRY 4250
NILTLMRMLS LKSLKKQMKK VKKMTVKDMV TAFFSSYWSI FMTLLHFVAS 4300
VFRGFFRIIC SLLLGGSLVE GAKKIKVAEL LANMPDPTQD EVRGDGEEGE 4350
RKPLEAALPS EDLTDLKELT EESDLLSDIF GLDLKREGGQ YKLIPHNPNA 4400
GLSDLMSNPV PMPEVQEKFQ EQKAKEEEKE EKEETKSEPE KAEGEDGEKE 4450
EKAKEDKGKQ KLRQLHTHRY GEPEVPESAF WKKIIAYQQK LLNYFARNFY 4500
NMRMLALFVA FAINFILLFY KVSTSSVVEG KELPTRSSSE NAKVTSLDSS 4550
SHRIIAVHYV LEESSGYMEP TLRILAILHT VISFFCIIGY YCLKVPLVIF 4600
KREKEVARKL EFDGLYITEQ PSEDDIKGQW DRLVINTQSF PNNYWDKFVK 4650
RKVMDKYGEF YGRDRISELL GMDKAALDFS DAREKKKPKK DSSLSAVLNS 4700
IDVKYQMWKL GVVFTDNSFL YLAWYMTMSV LGHYNNFFFA AHLLDIAMGF 4750
KTLRTILSSV THNGKQLVLT VGLLAVVVYL YTVVAFNFFR KFYNKSEDGD 4800
TPDMKCDDML TCYMFHMYVG VRAGGGIGDE IEDPAGDEYE IYRIIFDITF 4850
FFFVIVILLA IIQGLIIDAF GELRDQQEQV KEDMETKCFI CGIGNDYFDT 4900
VPHGFETHTL QEHNLANYLF FLMYLINKDE TEHTGQESYV WKMYQERCWE 4950
FFPAGDCFRK QYEDQLN 4967
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. Reason: Erroneous gene model prediction.
The sequence CAH71393.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAH73918.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI14440.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI15350.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI15936.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI22065.1 differs from that shown. Reason: Erroneous gene model prediction.

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. VSP_005953

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1037 – 10371L → P in CAA66975. 1 Publication
Sequence conflicti1037 – 10371L → P in CAC18855. 1 Publication
Sequence conflicti2785 – 27895WGWRI → RTMRT in CAA66975. 1 Publication
Sequence conflicti2785 – 27895WGWRI → RTMRT in CAC18855. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS55691.1. [Q92736-1 ]
PIRi S72269.
RefSeqi NP_001026.2. NM_001035.2. [Q92736-1 ]
XP_006711868.1. XM_006711805.1. [Q92736-2 ]
UniGenei Hs.109514.
Hs.738571.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JKQ X-ray 2.39 A 1-606 [» ]
ProteinModelPortali Q92736.
SMRi Q92736. Positions 10-544, 862-1068, 1082-1218, 2701-2905, 3581-3607, 4030-4086.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112174. 25 interactions.
DIPi DIP-38325N.
IntActi Q92736. 9 interactions.
MINTi MINT-1201008.
STRINGi 9606.ENSP00000355533.

Chemistry

GuidetoPHARMACOLOGYi 748.

Protein family/group databases

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

PTM databases

PhosphoSitei Q92736.

Polymorphism databases

DMDMi 308153558.

Proteomic databases

MaxQBi Q92736.
PaxDbi Q92736.
PRIDEi Q92736.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366574 ; ENSP00000355533 ; ENSG00000198626 . [Q92736-1 ]
GeneIDi 6262.
KEGGi hsa:6262.
UCSCi uc001hyl.1. human. [Q92736-1 ]

Organism-specific databases

CTDi 6262.
GeneCardsi GC01P237205.
GeneReviewsi RYR2.
HGNCi HGNC:10484. RYR2.
HPAi CAB006834.
HPA016697.
HPA020028.
MIMi 180902. gene.
600996. phenotype.
604772. phenotype.
neXtProti NX_Q92736.
Orphaneti 3286. 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.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247670.
HOGENOMi HOG000231428.
HOVERGENi HBG006699.
InParanoidi Q92736.
KOi K04962.
OrthoDBi EOG71K622.
PhylomeDBi Q92736.
TreeFami TF315244.

Enzyme and pathway databases

Reactomei REACT_160189. Stimuli-sensing channels.

Miscellaneous databases

ChiTaRSi RYR2. human.
GeneWikii Ryanodine_receptor_2.
GenomeRNAii 6262.
NextBioi 24325.
PROi Q92736.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q92736.
Bgeei Q92736.
CleanExi HS_RYR2.
Genevestigatori Q92736.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProi IPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
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.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view ]
PANTHERi PTHR13715. PTHR13715. 1 hit.
Pfami PF08709. 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 ]
PRINTSi PR00795. RYANODINER.
SMARTi SM00054. EFh. 2 hits.
SM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view ]
SUPFAMi SSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEi PS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view ]
ProtoNeti Search...

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.

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: September 3, 2014
This is version 160 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.

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

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