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Q92736

- RYR2_HUMAN

UniProt

Q92736 - RYR2_HUMAN

Protein

Ryanodine receptor 2

Gene

RYR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    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

    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 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

    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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 1 Publication
    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

    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.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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 42814281CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini4871 – 496797CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei4820 – 482910Pore-formingBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4282 – 430221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4504 – 452421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4580 – 460021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4730 – 475021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4769 – 478921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4850 – 487021HelicalSequence AnalysisAdd
    BLAST

    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

    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.
    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.

    « Hide

    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.

    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. 1 Publication
    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:
    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

    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: October 1, 2014
    This is version 161 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