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Q14571 (ITPR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ITPR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2701 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Homotetramer By similarity. Interacts with CABP1. Ref.4

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Isoform Short is found in skeletal muscle and heart.

Domain

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.

Post-translational modification

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

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.

Sequence similarities

Belongs to the InsP3 receptor family.

Contains 5 MIR domains.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
Ligand-gated ion channel
Receptor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

activation of phospholipase C activity

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular response to cAMP

Inferred from electronic annotation. Source: Ensembl

cellular response to ethanol

Inferred from electronic annotation. Source: Ensembl

energy reserve metabolic process

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

regulation of insulin secretion

Traceable author statement. Source: Reactome

response to hypoxia

Inferred from direct assay PubMed 19120137. Source: BHF-UCL

signal transduction

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell cortex

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 10828023. Source: BHF-UCL

platelet dense tubular network membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

sarcoplasmic reticulum membrane

Inferred from mutant phenotype PubMed 10828023. Source: BHF-UCL

   Molecular_functioncalcium ion transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Traceable author statement Ref.1. Source: ProtInc

phosphatidylinositol binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q14571-1)

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 Short (identifier: Q14571-2)

Also known as: TIPR;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27012701Inositol 1,4,5-trisphosphate receptor type 2
PRO_0000153924

Regions

Topological domain1 – 22272227Cytoplasmic Potential
Transmembrane2228 – 224821Helical; Potential
Topological domain2249 – 226012Extracellular Potential
Transmembrane2261 – 228121Helical; Potential
Topological domain2282 – 230726Cytoplasmic Potential
Transmembrane2308 – 232821Helical; Potential
Topological domain2329 – 235123Extracellular Potential
Transmembrane2352 – 237221Helical; Potential
Topological domain2373 – 239422Cytoplasmic Potential
Transmembrane2395 – 241521Helical; Potential
Topological domain2416 – 2521106Extracellular Potential
Transmembrane2522 – 254221Helical; Potential
Topological domain2543 – 2701159Cytoplasmic Potential
Domain112 – 16655MIR 1
Domain173 – 22351MIR 2
Domain231 – 28757MIR 3
Domain294 – 37279MIR 4
Domain378 – 43457MIR 5
Region265 – 2695Inositol 1,4,5-trisphosphate binding By similarity
Region507 – 5104Inositol 1,4,5-trisphosphate binding By similarity
Region567 – 5693Inositol 1,4,5-trisphosphate binding By similarity

Amino acid modifications

Modified residue9371Phosphoserine; by PKA By similarity
Modified residue11601Phosphoserine Ref.5
Modified residue26071Phosphotyrosine Potential

Natural variations

Alternative sequence176 – 1816IVVGDK → DASFWI in isoform Short.
VSP_002699
Alternative sequence182 – 27012520Missing in isoform Short.
VSP_002700
Natural variant4531A → V.
Corresponds to variant rs41453348 [ dbSNP | Ensembl ].
VAR_055963
Natural variant11431E → D.
Corresponds to variant rs16931091 [ dbSNP | Ensembl ].
VAR_055964
Natural variant18981A → V.
Corresponds to variant rs2230382 [ dbSNP | Ensembl ].
VAR_055965

Experimental info

Sequence conflict5971A → P in BAA05384. Ref.1
Sequence conflict10701P → A in BAA05384. Ref.1
Sequence conflict11781N → K in BAA05384. Ref.1

Sequences

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

Last modified September 22, 2009. Version 2.
Checksum: 373BA20228A159BC

FASTA2,701308,064
        10         20         30         40         50         60 
MTEKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV 

        70         80         90        100        110        120 
CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENKKL LGEIVKYSNV 

       130        140        150        160        170        180 
IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD 

       190        200        210        220        230        240 
KVVLMPVNAG QPLHASNIEL LDNPGCKEVN AVNCNTSWKI TLFMKYSSYR EDVLKGGDVV 

       250        260        270        280        290        300 
RLFHAEQEKF LTCDEYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN 

       310        320        330        340        350        360 
SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVRDGVPPTS KKKRQAGEKI MYTLVSVPHG 

       370        380        390        400        410        420 
NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TSIPIDTDEE RPVMLKIGTC 

       430        440        450        460        470        480 
QTKEDKEAFA IVSVPLSEVR DLDFANDANK VLATTVKKLE NGTITQNERR FVTKLLEDLI 

       490        500        510        520        530        540 
FFVADVPNNG QEVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED 

       550        560        570        580        590        600 
LGDQRYAPYK YMLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH 

       610        620        630        640        650        660 
NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NTTAIPVTQE LICKFMLSPG 

       670        680        690        700        710        720 
NADILIQTKV VSMQADNPME SSILSDDIDD EEVWLYWIDS NKEPHGKAIR HLAQEAKEGT 

       730        740        750        760        770        780 
KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCVSDESL PFDLRASFCR 

       790        800        810        820        830        840 
LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE 

       850        860        870        880        890        900 
YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM 

       910        920        930        940        950        960 
SSYFERLSKF QDGGNNVMRT IHGVGEMMTQ MVLSRGSIFP MSVPDVPPSI HPSKQGSPTE 

       970        980        990       1000       1010       1020 
HEDVTVMDTK LKIIEILQFI LSVRLDYRIS YMLSIYKKEF GEDNDNAETS ASGSPDTLLP 

      1030       1040       1050       1060       1070       1080 
SAIVPDIDEI AAQAETMFAG RKEKNPVQLD DEGGRTFLRV LIHLIMHDYP PLLSGALQLL 

      1090       1100       1110       1120       1130       1140 
FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSSNYENGE 

      1150       1160       1170       1180       1190       1200 
IGESQVKGGE EPIEESNILS PVQDGTKKPQ IDSNKSNNYR IVKEILIRLS KLCVQNKKCR 

      1210       1220       1230       1240       1250       1260 
NQHQRLLKNM GAHSVVLDLL QIPYEKNDEK MNEVMNLAHT FLQNFCRGNP QNQVLLHKHL 

      1270       1280       1290       1300       1310       1320 
NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD 

      1330       1340       1350       1360       1370       1380 
GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLHMMC SERDRGDESG PLAYHITLVE 

      1390       1400       1410       1420       1430       1440 
LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE 

      1450       1460       1470       1480       1490       1500 
IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADIFLEKCVT ESIMNIVSGF FNSPFSDNST 

      1510       1520       1530       1540       1550       1560 
SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRTL AEVAKNRGIA IPVDLDSQVN 

      1570       1580       1590       1600       1610       1620 
TLFMKSHSNM VQRAAMGWRL SARSGPRFKE ALGGPAWDYR NIIEKLQDVV ASLEHQFSPM 

      1630       1640       1650       1660       1670       1680 
MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE 

      1690       1700       1710       1720       1730       1740 
MLEKKDSFVE EGNTLRKILL NRYFKGDYSI GVNGHLSGAY SKTAQVGGSF SGQDSDKMGI 

      1750       1760       1770       1780       1790       1800 
SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGIFLGIA LLEGGNTQTQ YSFYQQLHEQ 

      1810       1820       1830       1840       1850       1860 
KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGNKKRDDD NELMTSGPRM RVRDSTLHLK 

      1870       1880       1890       1900       1910       1920 
EGMKGQLTEA SSATSKAYCV YRREMDPEID IMCTGPEAGN TEEKSAEEVT MSPAIAIMQP 

      1930       1940       1950       1960       1970       1980 
ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINEK 

      1990       2000       2010       2020       2030       2040 
NVALVNQNLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL 

      2050       2060       2070       2080       2090       2100 
KNNASKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DDEGGDDGVS 

      2110       2120       2130       2140       2150       2160 
PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPDEGDEALK YYANHTAQIE IVRHDRTMEQ 

      2170       2180       2190       2200       2210       2220 
IVFPVPNICE YLTRESKCRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRNNPALF 

      2230       2240       2250       2260       2270       2280 
WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PLFSVLLWIA VAICTSMLFF 

      2290       2300       2310       2320       2330       2340 
FSKPVGIRPF LVSIMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV 

      2350       2360       2370       2380       2390       2400 
ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV 

      2410       2420       2430       2440       2450       2460 
LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGSHQV PTMTLTTMME ACAKENCSPT 

      2470       2480       2490       2500       2510       2520 
IPASNTADEE YEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY 

      2530       2540       2550       2560       2570       2580 
DLLFYFIVII IVLNLIFGVI IDTFADLRSE KQKKEEILKT TCFICGLERD KFDNKTVSFE 

      2590       2600       2610       2620       2630       2640 
EHIKSEHNMW HYLYFIVLVK VKDPTEYTGP ESYVAQMIVE KNLDWFPRMR AMSLVSNEGD 

      2650       2660       2670       2680       2690       2700 
SEQNEIRSLQ EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP 


H 

« Hide

Isoform Short (TIPR) [UniParc].

Checksum: 146A91D12CE51863
Show »

FASTA18120,608

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS41764.1. [Q14571-1]
RefSeqNP_002214.2. NM_002223.2. [Q14571-1]
UniGeneHs.512235.

3D structure databases

ProteinModelPortalQ14571.
SMRQ14571. Positions 5-578.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109914. 2 interactions.
IntActQ14571. 2 interactions.
MINTMINT-157881.
STRING9606.ENSP00000370744.

Chemistry

BindingDBQ14571.
ChEMBLCHEMBL2111451.
GuidetoPHARMACOLOGY744.

PTM databases

PhosphoSiteQ14571.

Polymorphism databases

DMDM259016258.

Proteomic databases

MaxQBQ14571.
PaxDbQ14571.
PRIDEQ14571.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242737; ENSP00000242737; ENSG00000123104. [Q14571-2]
ENST00000381340; ENSP00000370744; ENSG00000123104. [Q14571-1]
GeneID3709.
KEGGhsa:3709.
UCSCuc001rhg.3. human. [Q14571-1]
uc001rhh.1. human. [Q14571-2]

Organism-specific databases

CTD3709.
GeneCardsGC12M026390.
H-InvDBHIX0036661.
HGNCHGNC:6181. ITPR2.
HPACAB022437.
MIM600144. gene.
neXtProtNX_Q14571.
PharmGKBPA29979.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280601.
HOGENOMHOG000007660.
HOVERGENHBG052158.
InParanoidQ14571.
KOK04959.
OMAQSAFRIY.
OrthoDBEOG76HQ0M.
PhylomeDBQ14571.
TreeFamTF312815.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressQ14571.
BgeeQ14571.
CleanExHS_ITPR2.
GenevestigatorQ14571.

Family and domain databases

Gene3D1.25.10.30. 2 hits.
InterProIPR016024. 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]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. 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]
PRINTSPR00779. INSP3RECEPTR.
SMARTSM00472. MIR. 4 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF48371. SSF48371. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITPR2. human.
GeneWikiITPR2.
GenomeRNAi3709.
NextBio14539.
PROQ14571.
SOURCESearch...

Entry information

Entry nameITPR2_HUMAN
AccessionPrimary (citable) accession number: Q14571
Secondary accession number(s): O94773
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 22, 2009
Last modified: July 9, 2014
This is version 142 of the entry and version 2 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

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 12

Human chromosome 12: entries, gene names and cross-references to MIM