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Q92736 (RYR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ryanodine receptor 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 names
Name:RYR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4967 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering 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. Ref.6 Ref.8

Subunit structure

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. Ref.6 Ref.7

Subcellular location

Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein Probable. Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic By similarity. Ref.6

Tissue specificity

Detected in heart muscle (at protein level). Heart muscle, brain (cerebellum and hippocampus) and placenta. Ref.5 Ref.6

Developmental stage

Expressed in myometrium during pregnancy. Ref.4

Induction

By TGFB1. Ref.4

Domain

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

Post-translational modification

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.

Involvement in disease

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. Ref.2

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. Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

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.

Sequence similarities

Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR2 subfamily. [View classification]

Contains 3 B30.2/SPRY domains.

Contains 5 MIR domains.

Sequence caution

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.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCardiomyopathy
Disease mutation
   DomainCoiled coil
Repeat
Transmembrane
Transmembrane helix
   LigandCalcium
Calmodulin-binding
   Molecular functionCalcium channel
Developmental protein
Ion channel
Ligand-gated ion channel
Receptor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

Purkinje myocyte to ventricular cardiac muscle cell signaling

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

calcium ion transport

Inferred from direct assay PubMed 17921453. Source: BHF-UCL

calcium ion transport into cytosol

Inferred from direct assay PubMed 17921453. Source: BHF-UCL

calcium-mediated signaling

Inferred from sequence or structural similarity. Source: UniProtKB

calcium-mediated signaling using intracellular calcium source

Inferred from direct assay PubMed 17921453. Source: BHF-UCL

canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

cardiac muscle contraction

Inferred from mutant phenotype Ref.6. Source: BHF-UCL

cardiac muscle hypertrophy

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

cell communication by electrical coupling involved in cardiac conduction

Inferred by curator. Source: BHF-UCL

cellular calcium ion homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to caffeine

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to epinephrine stimulus

Traceable author statement PubMed 23507255. Source: BHF-UCL

cytosolic calcium ion homeostasis

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

detection of calcium ion

Inferred from direct assay Ref.6. Source: BHF-UCL

embryonic heart tube morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of protein localization to endoplasmic reticulum

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

ion transmembrane transport

Traceable author statement. Source: Reactome

left ventricular cardiac muscle tissue morphogenesis

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

positive regulation of calcium-transporting ATPase activity

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

positive regulation of heart rate

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

positive regulation of ryanodine-sensitive calcium-release channel activity by adrenergic receptor signaling pathway involved in positive regulation of cardiac muscle contraction

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

positive regulation of sequestering of calcium ion

Inferred from direct assay PubMed 12443530PubMed 12919952. Source: BHF-UCL

regulation of cardiac muscle contraction

Inferred from mutant phenotype Ref.2. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

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

regulation of heart rate

Inferred from mutant phenotype Ref.2PubMed 12919952PubMed 15197150. Source: BHF-UCL

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 12443530PubMed 17921453. Source: BHF-UCL

release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from mutant phenotype PubMed 12919952. Source: BHF-UCL

response to caffeine

Inferred from direct assay PubMed 17921453. Source: BHF-UCL

response to hypoxia

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

response to redox state

Inferred from direct assay PubMed 19226252. Source: BHF-UCL

sarcoplasmic reticulum calcium ion transport

Traceable author statement PubMed 19095005. Source: BHF-UCL

transmembrane transport

Traceable author statement. Source: Reactome

type B pancreatic cell apoptotic process

Inferred from mutant phenotype PubMed 15044459. Source: BHF-UCL

ventricular cardiac muscle cell action potential

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

   Cellular_componentZ disc

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

calcium channel complex

Inferred from direct assay Ref.6PubMed 16213210. Source: BHF-UCL

junctional sarcoplasmic reticulum membrane

Traceable author statement PubMed 17569730. Source: BHF-UCL

membrane

Inferred from direct assay PubMed 12443530. Source: BHF-UCL

plasma membrane

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

protein complex

Inferred from direct assay PubMed 18468998. Source: MGI

sarcoplasmic reticulum

Inferred from direct assay Ref.6PubMed 12919952. Source: BHF-UCL

sarcoplasmic reticulum membrane

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

   Molecular_functioncalcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-induced calcium release activity

Inferred from direct assay PubMed 17921453. Source: BHF-UCL

calcium-release channel activity

Inferred from direct assay PubMed 17921453. Source: BHF-UCL

calmodulin binding

Inferred from mutant phenotype PubMed 19220289. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 16213210. Source: BHF-UCL

identical protein binding

Inferred from physical interaction Ref.6. Source: BHF-UCL

intracellular ligand-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

ion channel binding

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

protein binding

Inferred from physical interaction Ref.6PubMed 17921453. Source: UniProtKB

protein kinase A catalytic subunit binding

Inferred from direct assay Ref.6. Source: BHF-UCL

protein kinase A regulatory subunit binding

Inferred from direct assay Ref.6. Source: BHF-UCL

ryanodine-sensitive calcium-release channel activity

Inferred from direct assay PubMed 17921453. Source: BHF-UCL

suramin binding

Inferred from mutant phenotype PubMed 19220289. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q92736-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q92736-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 49674967Ryanodine receptor 2
PRO_0000219361

Regions

Topological domain1 – 42814281Cytoplasmic Potential
Transmembrane4282 – 430221Helical; Potential
Transmembrane4504 – 452421Helical; Potential
Transmembrane4580 – 460021Helical; Potential
Transmembrane4730 – 475021Helical; Potential
Transmembrane4769 – 478921Helical; Potential
Intramembrane4820 – 482910Pore-forming; By similarity
Transmembrane4850 – 487021Helical; Potential
Topological domain4871 – 496797Cytoplasmic Potential
Domain110 – 16556MIR 1
Domain172 – 21746MIR 2
Domain225 – 28056MIR 3
Domain286 – 34358MIR 4
Domain351 – 40858MIR 5
Domain599 – 809211B30.2/SPRY 1
Repeat853 – 9661141
Repeat967 – 10801142
Domain1025 – 1222198B30.2/SPRY 2
Domain1337 – 1562226B30.2/SPRY 3
Repeat2692 – 28101193
Repeat2812 – 29251144
Region853 – 292520734 X approximate repeats
Region3581 – 361030Interaction with CALM
Coiled coil4412 – 444534 Potential
Compositional bias4414 – 445542Glu-rich (acidic)

Amino acid modifications

Modified residue20311Phosphoserine; by PKA By similarity
Modified residue28081Phosphoserine; by CaMK2D and PKA Ref.6 Ref.8
Modified residue28141Phosphoserine; by CaMK2D Ref.8

Natural variations

Alternative sequence37151E → EVTGSQRSK in isoform 2.
VSP_005953
Natural variant1641P → S in CPVT1. Ref.18
VAR_044086
Natural variant1761R → Q in ARVD2 and CPVT1. Ref.2 Ref.16
VAR_044087
Natural variant4141R → L in CPVT1. Ref.18
VAR_044088
Natural variant4191I → F in CPVT1. Ref.18
VAR_044089
Natural variant4201R → W in CPVT1. Ref.16 Ref.21
Corresponds to variant rs190140598 [ dbSNP | Ensembl ].
VAR_044090
Natural variant4331L → P in ARVD2 and CPVT1. Ref.2 Ref.16
VAR_011395
Natural variant5071V → I.
Corresponds to variant rs16835270 [ dbSNP | Ensembl ].
VAR_044091
Natural variant18861G → S.
Corresponds to variant rs3766871 [ dbSNP | Ensembl ].
VAR_022078
Natural variant22461S → L in CPVT1. Ref.13 Ref.15 Ref.21
VAR_011396
Natural variant23061V → I in CPVT1. Ref.17
VAR_023694
Natural variant23111E → D in CPVT1. Ref.15
VAR_044092
Natural variant23281P → S in CPVT1. Ref.14
VAR_011397
Natural variant23861N → I in ARVD2 and CPVT1. Ref.2 Ref.16
VAR_011398
Natural variant23871A → P in CPVT1. Ref.20
VAR_044093
Natural variant23921Y → C in CPVT1. Ref.16
VAR_044094
Natural variant24031A → T in CPVT1. Ref.18
VAR_044095
Natural variant24741R → S in CPVT1. Ref.13 Ref.15
VAR_011399
Natural variant25041T → M in ARVD2 and CPVT1. Ref.2 Ref.16
VAR_044096
Natural variant29581Q → R. Ref.14
Corresponds to variant rs34967813 [ dbSNP | Ensembl ].
VAR_011590
Natural variant37781L → F in CPVT1. Ref.15
VAR_044097
Natural variant39461G → S in CPVT1. Ref.15
VAR_044098
Natural variant40971N → S in CPVT1. Ref.21
VAR_044099
Natural variant41041N → K in CPVT1. Ref.13 Ref.15
VAR_011400
Natural variant41461E → K in CPVT1. Ref.21
VAR_044100
Natural variant41581T → P in CPVT1. Ref.21
VAR_044101
Natural variant42011Q → R in CPVT1. Ref.14
VAR_011401
Natural variant44971R → C in CPVT1. Ref.13 Ref.15 Ref.21
VAR_011402
Natural variant44991F → C in CPVT1. Ref.18
VAR_044102
Natural variant45041M → I in CPVT1. Ref.19
VAR_044103
Natural variant45101A → T in CPVT1. Ref.18
VAR_044104
Natural variant46071A → P in CPVT1. Ref.20
VAR_044105
Natural variant46531V → F in CPVT1. Ref.14
VAR_011403
Natural variant46711G → R in CPVT1. Ref.18
VAR_044106
Natural variant47711V → I in CPVT1. Ref.15
VAR_044107
Natural variant48481I → V in CPVT1. Ref.18
VAR_044108
Natural variant48601A → 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. Ref.15 Ref.22
VAR_044109
Natural variant48671I → M in CPVT1. Ref.15
VAR_044110
Natural variant48801V → A in CPVT1. Ref.19
VAR_044111
Natural variant48951N → D in CPVT1. Ref.15
VAR_044112
Natural variant49021P → L in CPVT1. Ref.17
VAR_023695
Natural variant49501E → K in CPVT1. Ref.15
VAR_044113
Natural variant49591R → Q in CPVT1. Ref.17
VAR_023696

Experimental info

Mutagenesis28081S → A: Abolishes phosphorylation by PKA. Ref.6
Sequence conflict10371L → P in CAA66975. Ref.1
Sequence conflict10371L → P in CAC18855. Ref.2
Sequence conflict2785 – 27895WGWRI → RTMRT in CAA66975. Ref.1
Sequence conflict2785 – 27895WGWRI → RTMRT in CAC18855. Ref.2

Secondary structure

............................................................................................... 4967
Helix Strand Turn

Details...

Sequences

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

Last modified October 5, 2010. Version 3.
Checksum: 44984485F8677B42

FASTA4,967564,567
        10         20         30         40         50         60 
MADGGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP 

        70         80         90        100        110        120 
DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF MMKTAQGGGH RTLLYGHAIL 

       130        140        150        160        170        180 
LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ EDTTGEACWW TIHPASKQRS EGEKVRVGDD 

       190        200        210        220        230        240 
LILVSVSSER YLHLSYGNGS LHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH 

       250        260        270        280        290        300 
MDECLTVPSG EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV 

       310        320        330        340        350        360 
TTGKYLSLME DKNLLLMDKE KADVKSTAFT FRSSKEKLDV GVRKEVDGMG TSEIKYGDSV 

       370        380        390        400        410        420 
CYIQHVDTGL WLTYQSVDVK SVRMGSIQRK AIMHHEGHMD DGISLSRSQH EESRTARVIR 

       430        440        450        460        470        480 
STVFLFNRFI RGLDALSKKA KASTVDLPIE SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR 

       490        500        510        520        530        540 
ALKNRQNLFQ EEGMINLVLE CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL 

       550        560        570        580        590        600 
IRGNRKNCAQ FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL 

       610        620        630        640        650        660 
LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN HVSSMRPNIF 

       670        680        690        700        710        720 
LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST EGYSPYPGGG EEWGGNGVGD 

       730        740        750        760        770        780 
DLFSYGFDGL HLWSGCIART VSSPNQHLLR TDDVISCCLD LSAPSISFRI NGQPVQGMFE 

       790        800        810        820        830        840 
NFNIDGLFFP VVSFSAGIKV RFLLGGRHGE FKFLPPPGYA PCYEAVLPKE KLKVEHSREY 

       850        860        870        880        890        900 
KQERTYTRDL LGPTVSLTQA AFTPIPVDTS QIVLPPHLER IREKLAENIH ELWVMNKIEL 

       910        920        930        940        950        960 
GWQYGPVRDD NKRQHPCLVE FSKLPEQERN YNLQMSLETL KTLLALGCHV GISDEHAEDK 

       970        980        990       1000       1010       1020 
VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA ENAHNVWARD RIRQGWTYGI 

      1030       1040       1050       1060       1070       1080 
QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL REAVRTLLGY GYNLEAPDQD HAARAEVCSG 

      1090       1100       1110       1120       1130       1140 
TGERFRIFRA EKTYAVKAGR WYFEFETVTA GDMRVGWSRP GCQPDQELGS DERAFAFDGF 

      1150       1160       1170       1180       1190       1200 
KAQRWHQGNE HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG 

      1210       1220       1230       1240       1250       1260 
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW LSKRLPQFLQ 

      1270       1280       1290       1300       1310       1320 
VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNSNTDIM FYRLSMPIEC AEVFSKTVAG 

      1330       1340       1350       1360       1370       1380 
GLPGAGLFGP KNDLEDYDAD SDFEVLMKTA HGHLVPDRVD KDKEATKPEF NNHKDYAQEK 

      1390       1400       1410       1420       1430       1440 
PSRLKQRFLL RRTKPDYSTS HSARLTEDVL ADDRDDYDFL MQTSTYYYSV RIFPGQEPAN 

      1450       1460       1470       1480       1490       1500 
VWVGWITSDF HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR 

      1510       1520       1530       1540       1550       1560 
NNNGLEIGCV VDAASGLLTF IANGKELSTY YQVEPSTKLF PAVFAQATSP NVFQFELGRI 

      1570       1580       1590       1600       1610       1620 
KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRMP NQFLKVDVSR ISERQGWLVQ 

      1630       1640       1650       1660       1670       1680 
CLDPLQFMSL HIPEENRSVD ILELTEQEEL LKFHYHTLRL YSAVCALGNH RVAHALCSHV 

      1690       1700       1710       1720       1730       1740 
DEPQLLYAIE NKYMPGLLRA GYYDLLIDIH LSSYATARLM MNNEYIVPMT EETKSITLFP 

      1750       1760       1770       1780       1790       1800 
DENKKHGLPG IGLSTSLRPR MQFSSPSFVS ISNECYQYSP EFPLDILKSK TIQMLTEAVK 

      1810       1820       1830       1840       1850       1860 
EGSLHARDPV GGTTEFLFVP LIKLFYTLLI MGIFHNEDLK HILQLIEPSV FKEAATPEEE 

      1870       1880       1890       1900       1910       1920 
SDTLEKELSV DDAKLQGAGE EEAKGGKRPK EGLLQMKLPE PVKLQMCLLL QYLCDCQVRH 

      1930       1940       1950       1960       1970       1980 
RIEAIVAFSD DFVAKLQDNQ RFRYNEVMQA LNMSAALTAR KTKEFRSPPQ EQINMLLNFK 

      1990       2000       2010       2020       2030       2040 
DDKSECPCPE EIRDQLLDFH EDLMTHCGIE LDEDGSLDGN SDLTIRGRLL SLVEKVTYLK 

      2050       2060       2070       2080       2090       2100 
KKQAEKPVES DSKKSSTLQQ LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR 

      2110       2120       2130       2140       2150       2160 
ALPKTYTING VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM NNKVFYQHPN 

      2170       2180       2190       2200       2210       2220 
LMRALGMHET VMEVMVNVLG GGESKEITFP KMVANCCRFL CYFCRISRQN QKAMFDHLSY 

      2230       2240       2250       2260       2270       2280 
LLENSSVGLA SPAMRGSTPL DVAAASVMDN NELALALREP DLEKVVRYLA GCGLQSCQML 

      2290       2300       2310       2320       2330       2340 
VSKGYPDIGW NPVEGERYLD FLRFAVFCNG ESVEENANVV VRLLIRRPEC FGPALRGEGG 

      2350       2360       2370       2380       2390       2400 
NGLLAAMEEA IKIAEDPSRD GPSPNSGSSK TLDTEEEEDD TIHMGNAIMT FYSALIDLLG 

      2410       2420       2430       2440       2450       2460 
RCAPEMHLIH AGKGEAIRIR SILRSLIPLG DLVGVISIAF QMPTIAKDGN VVEPDMSAGF 

      2470       2480       2490       2500       2510       2520 
CPDHKAAMVL FLDRVYGIEV QDFLLHLLEV GFLPDLRAAA SLDTAALSAT DMALALNRYL 

      2530       2540       2550       2560       2570       2580 
CTAVLPLLTR CAPLFAGTEH HASLIDSLLH TVYRLSKGCS LTKAQRDSIE VCLLSICGQL 

      2590       2600       2610       2620       2630       2640 
RPSMMQHLLR RLVFDVPLLN EHAKMPLKLL TNHYERCWKY YCLPGGWGNF GAASEEELHL 

      2650       2660       2670       2680       2690       2700 
SRKLFWGIFD ALSQKKYEQE LFKLALPCLS AVAGALPPDY MESNYVSMME KQSSMDSEGN 

      2710       2720       2730       2740       2750       2760 
FNPQPVDTSN ITIPEKLEYF INKYAEHSHD KWSMDKLANG WIYGEIYSDS SKVQPLMKPY 

      2770       2780       2790       2800       2810       2820 
KLLSEKEKEI YRWPIKESLK TMLAWGWRIE RTREGDSMAL YNRTRRISQT SQVSVDAAHG 

      2830       2840       2850       2860       2870       2880 
YSPRAIDMSN VTLSRDLHAM AEMMAENYHN IWAKKKKMEL ESKGGGNHPL LVPYDTLTAK 

      2890       2900       2910       2920       2930       2940 
EKAKDREKAQ DILKFLQING YAVSRGFKDL ELDTPSIEKR FAYSFLQQLI RYVDEAHQYI 

      2950       2960       2970       2980       2990       3000 
LEFDGGSRGK GEHFPYEQEI KFFAKVVLPL IDQYFKNHRL YFLSAASRPL CSGGHASNKE 

      3010       3020       3030       3040       3050       3060 
KEMVTSLFCK LGVLVRHRIS LFGNDATSIV NCLHILGQTL DARTVMKTGL ESVKSALRAF 

      3070       3080       3090       3100       3110       3120 
LDNAAEDLEK TMENLKQGQF THTRNQPKGV TQIINYTTVA LLPMLSSLFE HIGQHQFGED 

      3130       3140       3150       3160       3170       3180 
LILEDVQVSC YRILTSLYAL GTSKSIYVER QRSALGECLA AFAGAFPVAF LETHLDKHNI 

      3190       3200       3210       3220       3230       3240 
YSIYNTKSSR ERAALSLPTN VEDVCPNIPS LEKLMEEIVE LAESGIRYTQ MPHVMEVILP 

      3250       3260       3270       3280       3290       3300 
MLCSYMSRWW EHGPENNPER AEMCCTALNS EHMNTLLGNI LKIIYNNLGI DEGAWMKRLA 

      3310       3320       3330       3340       3350       3360 
VFSQPIINKV KPQLLKTHFL PLMEKLKKKA ATVVSEEDHL KAEARGDMSE AELLILDEFT 

      3370       3380       3390       3400       3410       3420 
TLARDLYAFY PLLIRFVDYN RAKWLKEPNP EAEELFRMVA EVFIYWSKSH NFKREEQNFV 

      3430       3440       3450       3460       3470       3480 
VQNEINNMSF LITDTKSKMS KAAVSDQERK KMKRKGDRYS MQTSLIVAAL KRLLPIGLNI 

      3490       3500       3510       3520       3530       3540 
CAPGDQELIA LAKNRFSLKD TEDEVRDIIR SNIHLQGKLE DPAIRWQMAL YKDLPNRTDD 

      3550       3560       3570       3580       3590       3600 
TSDPEKTVER VLDIANVLFH LEQKSKRVGR RHYCLVEHPQ RSKKAVWHKL LSKQRKRAVV 

      3610       3620       3630       3640       3650       3660 
ACFRMAPLYN LPRHRAVNLF LQGYEKSWIE TEEHYFEDKL IEDLAKPGAE PPEEDEGTKR 

      3670       3680       3690       3700       3710       3720 
VDPLHQLILL FSRTALTEKC KLEEDFLYMA YADIMAKSCH DEEDDDGEEE VKSFEEKEME 

      3730       3740       3750       3760       3770       3780 
KQKLLYQQAR LHDRGAAEMV LQTISASKGE TGPMVAATLK LGIAILNGGN STVQQKMLDY 

      3790       3800       3810       3820       3830       3840 
LKEKKDVGFF QSLAGLMQSC SVLDLNAFER QNKAEGLGMV TEEGSGEKVL QDDEFTCDLF 

      3850       3860       3870       3880       3890       3900 
RFLQLLCEGH NSDFQNYLRT QTGNNTTVNI IISTVDYLLR VQESISDFYW YYSGKDVIDE 

      3910       3920       3930       3940       3950       3960 
QGQRNFSKAI QVAKQVFNTL TEYIQGPCTG NQQSLAHSRL WDAVVGFLHV FAHMQMKLSQ 

      3970       3980       3990       4000       4010       4020 
DSSQIELLKE LMDLQKDMVV MLLSMLEGNV VNGTIGKQMV DMLVESSNNV EMILKFFDMF 

      4030       4040       4050       4060       4070       4080 
LKLKDLTSSD TFKEYDPDGK GVISKRDFHK AMESHKHYTQ SETEFLLSCA ETDENETLDY 

      4090       4100       4110       4120       4130       4140 
EEFVKRFHEP AKDIGFNVAV LLTNLSEHMP NDTRLQTFLE LAESVLNYFQ PFLGRIEIMG 

      4150       4160       4170       4180       4190       4200 
SAKRIERVYF EISESSRTQW EKPQVKESKR QFIFDVVNEG GEKEKMELFV NFCEDTIFEM 

      4210       4220       4230       4240       4250       4260 
QLAAQISESD LNERSANKEE SEKERPEEQG PRMAFFSILT VRSALFALRY NILTLMRMLS 

      4270       4280       4290       4300       4310       4320 
LKSLKKQMKK VKKMTVKDMV TAFFSSYWSI FMTLLHFVAS VFRGFFRIIC SLLLGGSLVE 

      4330       4340       4350       4360       4370       4380 
GAKKIKVAEL LANMPDPTQD EVRGDGEEGE RKPLEAALPS EDLTDLKELT EESDLLSDIF 

      4390       4400       4410       4420       4430       4440 
GLDLKREGGQ YKLIPHNPNA GLSDLMSNPV PMPEVQEKFQ EQKAKEEEKE EKEETKSEPE 

      4450       4460       4470       4480       4490       4500 
KAEGEDGEKE EKAKEDKGKQ KLRQLHTHRY GEPEVPESAF WKKIIAYQQK LLNYFARNFY 

      4510       4520       4530       4540       4550       4560 
NMRMLALFVA FAINFILLFY KVSTSSVVEG KELPTRSSSE NAKVTSLDSS SHRIIAVHYV 

      4570       4580       4590       4600       4610       4620 
LEESSGYMEP TLRILAILHT VISFFCIIGY YCLKVPLVIF KREKEVARKL EFDGLYITEQ 

      4630       4640       4650       4660       4670       4680 
PSEDDIKGQW DRLVINTQSF PNNYWDKFVK RKVMDKYGEF YGRDRISELL GMDKAALDFS 

      4690       4700       4710       4720       4730       4740 
DAREKKKPKK DSSLSAVLNS IDVKYQMWKL GVVFTDNSFL YLAWYMTMSV LGHYNNFFFA 

      4750       4760       4770       4780       4790       4800 
AHLLDIAMGF KTLRTILSSV THNGKQLVLT VGLLAVVVYL YTVVAFNFFR KFYNKSEDGD 

      4810       4820       4830       4840       4850       4860 
TPDMKCDDML TCYMFHMYVG VRAGGGIGDE IEDPAGDEYE IYRIIFDITF FFFVIVILLA 

      4870       4880       4890       4900       4910       4920 
IIQGLIIDAF GELRDQQEQV KEDMETKCFI CGIGNDYFDT VPHGFETHTL QEHNLANYLF 

      4930       4940       4950       4960 
FLMYLINKDE TEHTGQESYV WKMYQERCWE FFPAGDCFRK QYEDQLN 

« Hide

Isoform 2 [UniParc].

Checksum: C24909FF9BC665B6
Show »

FASTA4,975565,411

References

« Hide 'large scale' references
[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. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Differential expression of ryanodine receptor RyR2 mRNA in the non-pregnant and pregnant human myometrium."
Awad S.S., Lamb H.K., Morgan J.M., Dunlop W., Gillespie J.I.
Biochem. J. 322:777-783(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-87 AND 533-681, DEVELOPMENTAL STAGE, INDUCTION BY TGFB1.
Tissue: Heart muscle and Myometrium.
[5]"Partial cloning and differential expression of ryanodine receptor/calcium-release channel genes in human tissues including the hippocampus and cerebellum."
Martin C., Chapman K.E., Seckl J.R., Ashley R.H.
Neuroscience 85:205-216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4292-4479, TISSUE SPECIFICITY.
Tissue: Cerebellum and Hippocampus.
[6]"PKA phosphorylation dissociates FKBP12.6 from the calcium release channel (ryanodine receptor): defective regulation in failing hearts."
Marx S.O., Reiken S., Hisamatsu Y., Jayaraman T., Burkhoff D., Rosemblit N., Marks A.R.
Cell 101:365-376(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH FKBP1B; PP1; PP2A AKAP6 AND PKA, INTERACTION WITH FKBP1B; PKA; PP1 AND PP2A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-2808, PHOSPHORYLATION AT SER-2808.
[7]"S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CALM AND S100A1.
[8]"CaMKII-dependent diastolic SR Ca2+ leak and elevated diastolic Ca2+ levels in right atrial myocardium of patients with atrial fibrillation."
Neef S., Dybkova N., Sossalla S., Ort K.R., Fluschnik N., Neumann K., Seipelt R., Schondube F.A., Hasenfuss G., Maier L.S.
Circ. Res. 106:1134-1144(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-2808 AND SER-2814.
[9]"Cardiac excitation-contraction coupling."
Bers D.M.
Nature 415:198-205(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[10]"Cardiac ryanodine receptor phosphorylation by CaM Kinase II: keeping the balance right."
Currie S.
Front. Biosci. 14:5134-5156(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"Modulation of ryanodine receptor Ca2+ channels."
Ozawa T.
Mol. Med. Report. 3:199-204(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[12]"Ryanodine receptors: structure, expression, molecular details, and function in calcium release."
Lanner J.T., Georgiou D.K., Joshi A.D., Hamilton S.L.
Cold Spring Harb. Perspect. Biol. 2:E3996-E3996(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Mutations in the cardiac ryanodine receptor gene (hRyR2) underlie catecholaminergic polymorphic ventricular tachycardia."
Priori S.G., Napolitano C., Tiso N., Memmi M., Vignati G., Bloise R., Sorrentino V.V., Danieli G.A.
Circulation 103:196-200(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VTSIP LEU-2246; SER-2474; LYS-4104 AND CYS-4497.
[14]"Mutations of the cardiac ryanodine receptor (RyR2) gene in familial polymorphic ventricular tachycardia."
Laitinen P.J., Brown K.M., Piippo K., Swan H., Devaney J.M., Brahmbhatt B., Donarum E.A., Marino M., Tiso N., Viitasalo M., Toivonen L., Stephan D.A., Kontula K.
Circulation 103:485-490(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT1 SER-2328; ARG-4201 AND PHE-4653, VARIANT ARG-2958.
[15]"Clinical and molecular characterization of patients with catecholaminergic polymorphic ventricular tachycardia."
Priori S.G., Napolitano C., Memmi M., Colombi B., Drago F., Gasparini M., DeSimone L., Coltorti F., Bloise R., Keegan R., Cruz Filho F.E.S., Vignati G., Benatar A., DeLogu A.
Circulation 106:69-74(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT1 LEU-2246; ASP-2311; SER-2474; PHE-3778; SER-3946; SER-3946; LYS-4104; CYS-4497; ILE-4771; GLY-4860; MET-4867; ASP-4895 AND LYS-4950.
[16]"Screening for ryanodine receptor type 2 mutations in families with effort-induced polymorphic ventricular arrhythmias and sudden death: early diagnosis of asymptomatic carriers."
Bauce B., Rampazzo A., Basso C., Bagattin A., Daliento L., Tiso N., Turrini P., Thiene G., Danieli G.A., Nava A.
J. Am. Coll. Cardiol. 40:341-349(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT1 GLN-176; TRP-420; PRO-433; ILE-2386; CYS-2392 AND MET-2504.
[17]"Molecular genetics of exercise-induced polymorphic ventricular tachycardia: identification of three novel cardiac ryanodine receptor mutations and two common calsequestrin 2 amino-acid polymorphisms."
Laitinen P.J., Swan H., Kontula K.
Eur. J. Hum. Genet. 11:888-891(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VTSIP ILE-2306; LEU-4902 AND GLN-4959.
[18]"Spectrum and frequency of cardiac channel defects in swimming-triggered arrhythmia syndromes."
Choi G., Kopplin L.J., Tester D.J., Will M.L., Haglund C.M., Ackerman M.J.
Circulation 110:2119-2124(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT1 SER-164; LEU-414; PHE-419; THR-2403; CYS-4499; THR-4510; ARG-4671 AND VAL-4848.
[19]"Gene symbol: RYR2. Disease: effort-induced polymorphic ventricular arrhythmias."
Bagattin A., Veronese C., Rampazzo A., Danieli G.A.
Hum. Genet. 114:404-404(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT1 ILE-4504 AND ALA-4880.
[20]"Gene symbol: RYR2. Disease: effort-induced polymorphic ventricular arrhythmias."
Bagattin A., Veronese C., Rampazzo A., Danieli G.A.
Hum. Genet. 114:405-405(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT1 PRO-2387 AND PRO-4607.
[21]"Targeted mutational analysis of the RyR2-encoded cardiac ryanodine receptor in sudden unexplained death: a molecular autopsy of 49 medical examiner/coroner's cases."
Tester D.J., Spoon D.B., Valdivia H.H., Makielski J.C., Ackerman M.J.
Mayo Clin. Proc. 79:1380-1384(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CPVT1 TRP-420; LEU-2246; SER-4097; LYS-4146; PRO-4158 AND CYS-4497.
[22]"Loss of luminal Ca(2+) activation in the cardiac ryanodine receptor is associated with ventricular fibrillation and sudden death."
Jiang D., Chen W., Wang R., Zhang L., Chen S.R.W.
Proc. Natl. Acad. Sci. U.S.A. 104:18309-18314(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CPVT1 GLY-4860.
+Additional computationally mapped references.

Web resources

Wikipedia

Ryanodine receptor entry

Wikipedia

RYR2 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98330 mRNA. Translation: CAA66975.1.
AJ300340 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , AL356773, AL359924, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAH71369.1. Sequence problems.
AL445473 expand/collapse EMBL AC list , AL356773, AL359924, AL365332, AL391809, AL442065, AL513130 Genomic DNA. Translation: CAH71393.1. Sequence problems.
AL356773 expand/collapse EMBL AC list , AL359924, AL365332, AL391809, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAH73918.1. Sequence problems.
AL391809 expand/collapse EMBL AC list , AL356773, AL359924, AL365332, AL442065, AL445473, AL513130 Genomic DNA. Translation: CAI14440.1. Sequence problems.
AL442065 expand/collapse EMBL AC list , AL356773, AL359924, AL365332, AL391809, AL445473, AL513130 Genomic DNA. Translation: CAI15350.1. Sequence problems.
AL513130 expand/collapse EMBL AC list , AL356773, AL359924, AL365332, AL391809, AL442065, AL445473 Genomic DNA. Translation: CAI15936.1. Sequence problems.
AL359924 expand/collapse EMBL AC list , 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.
CCDSCCDS55691.1. [Q92736-1]
PIRS72269.
RefSeqNP_001026.2. NM_001035.2. [Q92736-1]
XP_006711868.1. XM_006711805.1. [Q92736-2]
UniGeneHs.109514.
Hs.738571.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4JKQX-ray2.39A1-606[»]
ProteinModelPortalQ92736.
SMRQ92736. Positions 10-544, 862-1068, 1082-1218, 2701-2905, 3581-3607, 4030-4086.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112174. 25 interactions.
DIPDIP-38325N.
IntActQ92736. 9 interactions.
MINTMINT-1201008.
STRING9606.ENSP00000355533.

Chemistry

GuidetoPHARMACOLOGY748.

Protein family/group databases

TCDB1.A.3.1.1. the ryanodine-inositol 1,4,5-triphosphate receptor ca(2+) channel (rir-cac) family.

PTM databases

PhosphoSiteQ92736.

Polymorphism databases

DMDM308153558.

Proteomic databases

MaxQBQ92736.
PaxDbQ92736.
PRIDEQ92736.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366574; ENSP00000355533; ENSG00000198626. [Q92736-1]
GeneID6262.
KEGGhsa:6262.
UCSCuc001hyl.1. human. [Q92736-1]

Organism-specific databases

CTD6262.
GeneCardsGC01P237205.
GeneReviewsRYR2.
HGNCHGNC:10484. RYR2.
HPACAB006834.
HPA016697.
HPA020028.
MIM180902. gene.
600996. phenotype.
604772. phenotype.
neXtProtNX_Q92736.
Orphanet3286. 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.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247670.
HOGENOMHOG000231428.
HOVERGENHBG006699.
InParanoidQ92736.
KOK04962.
OrthoDBEOG71K622.
PhylomeDBQ92736.
TreeFamTF315244.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ92736.
BgeeQ92736.
CleanExHS_RYR2.
GenevestigatorQ92736.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR011992. EF-hand-dom_pair.
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]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF06459. RR_TM4-6. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
PF02026. RyR. 4 hits.
PF00622. SPRY. 3 hits.
[Graphical view]
PRINTSPR00795. RYANODINER.
SMARTSM00054. EFh. 2 hits.
SM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRYR2. human.
GeneWikiRyanodine_receptor_2.
GenomeRNAi6262.
NextBio24325.
PROQ92736.
SOURCESearch...

Entry information

Entry nameRYR2_HUMAN
AccessionPrimary (citable) accession number: Q92736
Secondary accession number(s): Q15411, Q546N8, Q5T3P2
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM