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Q14571

- ITPR2_HUMAN

UniProt

Q14571 - ITPR2_HUMAN

Protein

Inositol 1,4,5-trisphosphate receptor type 2

Gene

ITPR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (22 Sep 2009)
      Previous versions | rss
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    Functioni

    Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium. This release is regulated by cAMP both dependently and independently of PKA By similarity.By similarity

    GO - Molecular functioni

    1. calcium ion transmembrane transporter activity Source: ProtInc
    2. inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: ProtInc
    3. phosphatidylinositol binding Source: Ensembl

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. blood coagulation Source: Reactome
    3. cellular response to cAMP Source: Ensembl
    4. cellular response to ethanol Source: Ensembl
    5. energy reserve metabolic process Source: Reactome
    6. epidermal growth factor receptor signaling pathway Source: Reactome
    7. Fc-epsilon receptor signaling pathway Source: Reactome
    8. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    9. fibroblast growth factor receptor signaling pathway Source: Reactome
    10. innate immune response Source: Reactome
    11. neurotrophin TRK receptor signaling pathway Source: Reactome
    12. platelet activation Source: Reactome
    13. regulation of insulin secretion Source: Reactome
    14. response to hypoxia Source: BHF-UCL
    15. signal transduction Source: Reactome
    16. small molecule metabolic process Source: Reactome
    17. transport Source: ProtInc

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Calcium transport, Ion transport, Transport

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_111064. DAG and IP3 signaling.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_15426. PLC beta mediated events.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_162. Elevation of cytosolic Ca2+ levels.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_172761. Ca2+ pathway.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18325. Regulation of insulin secretion.
    REACT_2202. Effects of PIP2 hydrolysis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol 1,4,5-trisphosphate receptor type 2
    Alternative name(s):
    IP3 receptor isoform 2
    Short name:
    IP3R 2
    Short name:
    InsP3R2
    Type 2 inositol 1,4,5-trisphosphate receptor
    Short name:
    Type 2 InsP3 receptor
    Gene namesi
    Name:ITPR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6181. ITPR2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell cortex Source: Ensembl
    2. endoplasmic reticulum membrane Source: Reactome
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane Source: UniProtKB
    5. plasma membrane Source: BHF-UCL
    6. platelet dense tubular network membrane Source: Reactome
    7. receptor complex Source: MGI
    8. sarcoplasmic reticulum membrane Source: BHF-UCL

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29979.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 27012701Inositol 1,4,5-trisphosphate receptor type 2PRO_0000153924Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei937 – 9371Phosphoserine; by PKABy similarity
    Modified residuei1160 – 11601Phosphoserine1 Publication
    Modified residuei2607 – 26071PhosphotyrosineSequence Analysis

    Post-translational modificationi

    Phosphorylation by cAMP-dependent PKA on Ser-937 increases calcium release.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14571.
    PaxDbiQ14571.
    PRIDEiQ14571.

    PTM databases

    PhosphoSiteiQ14571.

    Expressioni

    Tissue specificityi

    Isoform Short is found in skeletal muscle and heart.

    Gene expression databases

    ArrayExpressiQ14571.
    BgeeiQ14571.
    CleanExiHS_ITPR2.
    GenevestigatoriQ14571.

    Organism-specific databases

    HPAiCAB022437.

    Interactioni

    Subunit structurei

    Homotetramer By similarity. Interacts with CABP1.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi109914. 2 interactions.
    IntActiQ14571. 2 interactions.
    MINTiMINT-157881.
    STRINGi9606.ENSP00000370744.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14571.
    SMRiQ14571. Positions 5-578.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 22272227CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2249 – 226012ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2282 – 230726CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2329 – 235123ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2373 – 239422CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini2416 – 2521106ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini2543 – 2701159CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2228 – 224821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2261 – 228121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2308 – 232821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2352 – 237221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2395 – 241521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei2522 – 254221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini112 – 16655MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 22351MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini231 – 28757MIR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini294 – 37279MIR 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 43457MIR 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni265 – 2695Inositol 1,4,5-trisphosphate bindingBy similarity
    Regioni507 – 5104Inositol 1,4,5-trisphosphate bindingBy similarity
    Regioni567 – 5693Inositol 1,4,5-trisphosphate bindingBy similarity

    Domaini

    The receptor contains a calcium channel in its C-terminal extremity. Its large N-terminal cytoplasmic region has the ligand-binding site in the N-terminus and modulatory sites in the middle portion immediately upstream of the channel region.

    Sequence similaritiesi

    Belongs to the InsP3 receptor family.Curated
    Contains 5 MIR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG280601.
    HOGENOMiHOG000007660.
    HOVERGENiHBG052158.
    InParanoidiQ14571.
    KOiK04959.
    OMAiQSAFRIY.
    OrthoDBiEOG76HQ0M.
    PhylomeDBiQ14571.
    TreeFamiTF312815.

    Family and domain databases

    Gene3Di1.25.10.30. 2 hits.
    InterProiIPR016024. ARM-type_fold.
    IPR014821. Ins145_P3_rcpt.
    IPR000493. InsP3_rcpt-bd.
    IPR005821. Ion_trans_dom.
    IPR016093. MIR_motif.
    IPR013662. RIH_assoc-dom.
    IPR000699. RIH_dom.
    IPR015925. Ryanodine_recept-rel.
    [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.
    PF01365. RYDR_ITPR. 2 hits.
    [Graphical view]
    PRINTSiPR00779. INSP3RECEPTR.
    SMARTiSM00472. MIR. 4 hits.
    [Graphical view]
    SUPFAMiSSF100909. SSF100909. 2 hits.
    SSF48371. SSF48371. 3 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEiPS50919. MIR. 5 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q14571-1) [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

    MTEKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLANPP     50
    KKFRDCLFKV CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ 100
    KQNESENKKL LGEIVKYSNV IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS 150
    LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD KVVLMPVNAG QPLHASNIEL 200
    LDNPGCKEVN AVNCNTSWKI TLFMKYSSYR EDVLKGGDVV RLFHAEQEKF 250
    LTCDEYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN 300
    SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVRDGVPPTS KKKRQAGEKI 350
    MYTLVSVPHG NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS 400
    TSIPIDTDEE RPVMLKIGTC QTKEDKEAFA IVSVPLSEVR DLDFANDANK 450
    VLATTVKKLE NGTITQNERR FVTKLLEDLI FFVADVPNNG QEVLDVVITK 500
    PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED LGDQRYAPYK 550
    YMLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH 600
    NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NTTAIPVTQE 650
    LICKFMLSPG NADILIQTKV VSMQADNPME SSILSDDIDD EEVWLYWIDS 700
    NKEPHGKAIR HLAQEAKEGT KADLEVLTYY RYQLNLFARM CLDRQYLAIN 750
    QISTQLSVDL ILRCVSDESL PFDLRASFCR LMLHMHVDRD PQESVVPVRY 800
    ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE YLKEVVNQPF 850
    PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM 900
    SSYFERLSKF QDGGNNVMRT IHGVGEMMTQ MVLSRGSIFP MSVPDVPPSI 950
    HPSKQGSPTE HEDVTVMDTK LKIIEILQFI LSVRLDYRIS YMLSIYKKEF 1000
    GEDNDNAETS ASGSPDTLLP SAIVPDIDEI AAQAETMFAG RKEKNPVQLD 1050
    DEGGRTFLRV LIHLIMHDYP PLLSGALQLL FKHFSQRAEV LQAFKQVQLL 1100
    VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSSNYENGE IGESQVKGGE 1150
    EPIEESNILS PVQDGTKKPQ IDSNKSNNYR IVKEILIRLS KLCVQNKKCR 1200
    NQHQRLLKNM GAHSVVLDLL QIPYEKNDEK MNEVMNLAHT FLQNFCRGNP 1250
    QNQVLLHKHL NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI 1300
    ETHGRHVEYL RFLQTIVKAD GKYVKKCQDM VMTELINGGE DVLIFYNDRA 1350
    SFPILLHMMC SERDRGDESG PLAYHITLVE LLAACTEGKN VYTEIKCNSL 1400
    LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE IYTSNHIWKL 1450
    FENFLVDMAR VCNTTTDRKH ADIFLEKCVT ESIMNIVSGF FNSPFSDNST 1500
    SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRTL AEVAKNRGIA 1550
    IPVDLDSQVN TLFMKSHSNM VQRAAMGWRL SARSGPRFKE ALGGPAWDYR 1600
    NIIEKLQDVV ASLEHQFSPM MQAEFSVLVD VLYSPELLFP EGSDARIRCG 1650
    AFMSKLINHT KKLMEKEEKL CIKILQTLRE MLEKKDSFVE EGNTLRKILL 1700
    NRYFKGDYSI GVNGHLSGAY SKTAQVGGSF SGQDSDKMGI SMSDIQCLLD 1750
    KEGASELVID VIVNTKNDRI FSEGIFLGIA LLEGGNTQTQ YSFYQQLHEQ 1800
    KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGNKKRDDD NELMTSGPRM 1850
    RVRDSTLHLK EGMKGQLTEA SSATSKAYCV YRREMDPEID IMCTGPEAGN 1900
    TEEKSAEEVT MSPAIAIMQP ILRFLQLLCE NHNRELQNFL RNQNNKTNYN 1950
    LVCETLQFLD CICGSTTGGL GLLGLYINEK NVALVNQNLE SLTEYCQGPC 2000
    HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL KNNASKLLLA 2050
    IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DDEGGDDGVS 2100
    PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPDEGDEALK YYANHTAQIE 2150
    IVRHDRTMEQ IVFPVPNICE YLTRESKCRV FNTTERDEQG SKVNDFFQQT 2200
    EDLYNEMKWQ KKIRNNPALF WFSRHISLWG SISFNLAVFI NLAVALFYPF 2250
    GDDGDEGTLS PLFSVLLWIA VAICTSMLFF FSKPVGIRPF LVSIMLRSIY 2300
    TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV ILDMAFLYHV 2350
    AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV 2400
    LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGSHQV PTMTLTTMME 2450
    ACAKENCSPT IPASNTADEE YEDGIERTCD TLLMCIVTVL NQGLRNGGGV 2500
    GDVLRRPSKD EPLFAARVVY DLLFYFIVII IVLNLIFGVI IDTFADLRSE 2550
    KQKKEEILKT TCFICGLERD KFDNKTVSFE EHIKSEHNMW HYLYFIVLVK 2600
    VKDPTEYTGP ESYVAQMIVE KNLDWFPRMR AMSLVSNEGD SEQNEIRSLQ 2650
    EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP 2700
    H 2701
    Length:2,701
    Mass (Da):308,064
    Last modified:September 22, 2009 - v2
    Checksum:i373BA20228A159BC
    GO
    Isoform Short (identifier: Q14571-2) [UniParc]FASTAAdd to Basket

    Also known as: TIPR

    The sequence of this isoform differs from the canonical sequence as follows:
         176-181: IVVGDK → DASFWI
         182-2701: Missing.

    Show »
    Length:181
    Mass (Da):20,608
    Checksum:i146A91D12CE51863
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti597 – 5971A → P in BAA05384. (PubMed:8081734)Curated
    Sequence conflicti1070 – 10701P → A in BAA05384. (PubMed:8081734)Curated
    Sequence conflicti1178 – 11781N → K in BAA05384. (PubMed:8081734)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti453 – 4531A → V.
    Corresponds to variant rs41453348 [ dbSNP | Ensembl ].
    VAR_055963
    Natural varianti1143 – 11431E → D.
    Corresponds to variant rs16931091 [ dbSNP | Ensembl ].
    VAR_055964
    Natural varianti1898 – 18981A → V.
    Corresponds to variant rs2230382 [ dbSNP | Ensembl ].
    VAR_055965

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei176 – 1816IVVGDK → DASFWI in isoform Short. 1 PublicationVSP_002699
    Alternative sequencei182 – 27012520Missing in isoform Short. 1 PublicationVSP_002700Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26350 mRNA. Translation: BAA05384.1.
    AB012610 mRNA. Translation: BAA33961.1.
    AC023051 Genomic DNA. No translation available.
    AC023425 Genomic DNA. No translation available.
    AC024093 Genomic DNA. No translation available.
    AC024145 Genomic DNA. No translation available.
    AC055720 Genomic DNA. No translation available.
    CCDSiCCDS41764.1. [Q14571-1]
    RefSeqiNP_002214.2. NM_002223.2. [Q14571-1]
    UniGeneiHs.512235.

    Genome annotation databases

    EnsembliENST00000242737; ENSP00000242737; ENSG00000123104. [Q14571-2]
    ENST00000381340; ENSP00000370744; ENSG00000123104. [Q14571-1]
    GeneIDi3709.
    KEGGihsa:3709.
    UCSCiuc001rhg.3. human. [Q14571-1]
    uc001rhh.1. human. [Q14571-2]

    Polymorphism databases

    DMDMi259016258.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26350 mRNA. Translation: BAA05384.1 .
    AB012610 mRNA. Translation: BAA33961.1 .
    AC023051 Genomic DNA. No translation available.
    AC023425 Genomic DNA. No translation available.
    AC024093 Genomic DNA. No translation available.
    AC024145 Genomic DNA. No translation available.
    AC055720 Genomic DNA. No translation available.
    CCDSi CCDS41764.1. [Q14571-1 ]
    RefSeqi NP_002214.2. NM_002223.2. [Q14571-1 ]
    UniGenei Hs.512235.

    3D structure databases

    ProteinModelPortali Q14571.
    SMRi Q14571. Positions 5-578.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109914. 2 interactions.
    IntActi Q14571. 2 interactions.
    MINTi MINT-157881.
    STRINGi 9606.ENSP00000370744.

    Chemistry

    BindingDBi Q14571.
    ChEMBLi CHEMBL2111451.
    GuidetoPHARMACOLOGYi 744.

    PTM databases

    PhosphoSitei Q14571.

    Polymorphism databases

    DMDMi 259016258.

    Proteomic databases

    MaxQBi Q14571.
    PaxDbi Q14571.
    PRIDEi Q14571.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000242737 ; ENSP00000242737 ; ENSG00000123104 . [Q14571-2 ]
    ENST00000381340 ; ENSP00000370744 ; ENSG00000123104 . [Q14571-1 ]
    GeneIDi 3709.
    KEGGi hsa:3709.
    UCSCi uc001rhg.3. human. [Q14571-1 ]
    uc001rhh.1. human. [Q14571-2 ]

    Organism-specific databases

    CTDi 3709.
    GeneCardsi GC12M026390.
    H-InvDB HIX0036661.
    HGNCi HGNC:6181. ITPR2.
    HPAi CAB022437.
    MIMi 600144. gene.
    neXtProti NX_Q14571.
    PharmGKBi PA29979.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG280601.
    HOGENOMi HOG000007660.
    HOVERGENi HBG052158.
    InParanoidi Q14571.
    KOi K04959.
    OMAi QSAFRIY.
    OrthoDBi EOG76HQ0M.
    PhylomeDBi Q14571.
    TreeFami TF312815.

    Enzyme and pathway databases

    Reactomei REACT_111064. DAG and IP3 signaling.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_15426. PLC beta mediated events.
    REACT_160158. Role of phospholipids in phagocytosis.
    REACT_162. Elevation of cytosolic Ca2+ levels.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_172761. Ca2+ pathway.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_18325. Regulation of insulin secretion.
    REACT_2202. Effects of PIP2 hydrolysis.

    Miscellaneous databases

    ChiTaRSi ITPR2. human.
    GeneWikii ITPR2.
    GenomeRNAii 3709.
    NextBioi 14539.
    PROi Q14571.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14571.
    Bgeei Q14571.
    CleanExi HS_ITPR2.
    Genevestigatori Q14571.

    Family and domain databases

    Gene3Di 1.25.10.30. 2 hits.
    InterProi IPR016024. ARM-type_fold.
    IPR014821. Ins145_P3_rcpt.
    IPR000493. InsP3_rcpt-bd.
    IPR005821. Ion_trans_dom.
    IPR016093. MIR_motif.
    IPR013662. RIH_assoc-dom.
    IPR000699. RIH_dom.
    IPR015925. Ryanodine_recept-rel.
    [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.
    PF01365. RYDR_ITPR. 2 hits.
    [Graphical view ]
    PRINTSi PR00779. INSP3RECEPTR.
    SMARTi SM00472. MIR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF100909. SSF100909. 2 hits.
    SSF48371. SSF48371. 3 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEi PS50919. MIR. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of human type 2 and type 3 inositol 1,4,5-trisphosphate receptors."
      Yamamoto-Hino M., Sugiyama T., Hikiti K., Mattei M.-G., Hasegawa K., Sekine S., Sakurada K., Miyawaki A., Furuichi T., Hasegawa M., Mikoshiba K.
      Recept. Channels 2:9-22(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    2. "Muscle-specific mRNA isoform encodes a protein composed mainly of the N-terminal 175 residues of type 2 Ins(1,4,5)P3 receptor."
      Futatsugi A., Kuwajima G., Mikoshiba K.
      Biochem. J. 334:559-563(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
      Tissue: Heart.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca(2+) release channels."
      Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F., Foskett J.K.
      Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CABP1.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiITPR2_HUMAN
    AccessioniPrimary (citable) accession number: Q14571
    Secondary accession number(s): O94773
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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

    Calcium appears to inhibit ligand binding to the receptor, most probably by interacting with a distinct calcium-binding protein which then inhibits the receptor.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3