Q14571 (ITPR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

ITPR2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2701 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Calcium transport Ion transport Transport
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium
Molecular function	Calcium channel Ion channel Ligand-gated ion channel Receptor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of phospholipase C activity Traceable author statement. Source: Reactome cellular response to cAMP Inferred from electronic annotation. Source: Compara cellular response to ethanol Inferred from electronic annotation. Source: Compara 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 nerve growth factor 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 small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	cell cortex Inferred from electronic annotation. Source: Compara integral to 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 sarcoplasmic reticulum membrane Inferred from mutant phenotype PubMed 10828023. Source: BHF-UCL
Molecular_function	inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Traceable author statement Ref.1. Source: ProtInc phosphatidylinositol binding Inferred from electronic annotation. Source: Compara
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2701	2701	Inositol 1,4,5-trisphosphate receptor type 2		PRO_0000153924
Regions
	Topological domain	1 – 2227	2227	Cytoplasmic Potential
	Transmembrane	2228 – 2248	21	Helical; Potential
	Topological domain	2249 – 2260	12	Extracellular Potential
	Transmembrane	2261 – 2281	21	Helical; Potential
	Topological domain	2282 – 2307	26	Cytoplasmic Potential
	Transmembrane	2308 – 2328	21	Helical; Potential
	Topological domain	2329 – 2351	23	Extracellular Potential
	Transmembrane	2352 – 2372	21	Helical; Potential
	Topological domain	2373 – 2394	22	Cytoplasmic Potential
	Transmembrane	2395 – 2415	21	Helical; Potential
	Topological domain	2416 – 2521	106	Extracellular Potential
	Transmembrane	2522 – 2542	21	Helical; Potential
	Topological domain	2543 – 2701	159	Cytoplasmic Potential
	Domain	112 – 166	55	MIR 1
	Domain	173 – 223	51	MIR 2
	Domain	231 – 287	57	MIR 3
	Domain	294 – 372	79	MIR 4
	Domain	378 – 434	57	MIR 5
	Region	265 – 269	5	Inositol 1,4,5-trisphosphate binding By similarity
	Region	507 – 510	4	Inositol 1,4,5-trisphosphate binding By similarity
	Region	567 – 569	3	Inositol 1,4,5-trisphosphate binding By similarity
Amino acid modifications
	Modified residue	937	1	Phosphoserine; by PKA By similarity
	Modified residue	1160	1	Phosphoserine Ref.5
	Modified residue	1709	1	Phosphoserine By similarity
	Modified residue	2607	1	Phosphotyrosine Potential
Natural variations
	Alternative sequence	176 – 181	6	IVVGDK → DASFWI in isoform Short.		VSP_002699
	Alternative sequence	182 – 2701	2520	Missing in isoform Short.		VSP_002700
	Natural variant	453	1	A → V. Corresponds to variant rs41453348 [ dbSNP | Ensembl ].		VAR_055963
	Natural variant	1143	1	E → D. Corresponds to variant rs16931091 [ dbSNP | Ensembl ].		VAR_055964
	Natural variant	1898	1	A → V. Corresponds to variant rs2230382 [ dbSNP | Ensembl ].		VAR_055965
Experimental info
	Sequence conflict	597	1	A → P in BAA05384. Ref.1
	Sequence conflict	1070	1	P → A in BAA05384. Ref.1
	Sequence conflict	1178	1	N → K in BAA05384. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified September 22, 2009. Version 2. Checksum: 373BA20228A159BC	FASTA	2,701	308,064
	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
	Isoform Short (TIPR) [UniParc]. Checksum: 146A91D12CE51863	FASTA	181	20,608
	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 SEGDNDASFW I

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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.
IPI	IPI00031545. IPI00218668.
RefSeq	NP_002214.2. NM_002223.2.
UniGene	Hs.512235.
3D structure databases
ProteinModelPortal	Q14571.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14571. 1 interaction.
MINT	MINT-157881.
STRING	9606.ENSP00000370744.
PTM databases
PhosphoSite	Q14571.
Polymorphism databases
DMDM	259016258.
Proteomic databases
PaxDb	Q14571.
PRIDE	Q14571.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000242737; ENSP00000242737; ENSG00000123104. ENST00000381340; ENSP00000370744; ENSG00000123104.
GeneID	3709.
KEGG	hsa:3709.
UCSC	uc001rhg.3. human. uc001rhh.1. human.
Organism-specific databases
CTD	3709.
GeneCards	GC12M026390.
H-InvDB	HIX0036661.
HGNC	HGNC:6181. ITPR2.
HPA	CAB022437.
MIM	600144. gene.
neXtProt	NX_Q14571.
PharmGKB	PA29979.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG280601.
HOGENOM	HOG000007660.
HOVERGEN	HBG052158.
InParanoid	Q14571.
KO	K04959.
OMA	QSAFRIY.
OrthoDB	EOG4GQQ42.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_116125. Disease. REACT_604. Hemostasis. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q14571.
Bgee	Q14571.
CleanEx	HS_ITPR2.
Genevestigator	Q14571.
GermOnline	ENSG00000123104. Homo sapiens.
Family and domain databases
InterPro	IPR000699. Ca-rel_channel. IPR014821. Ins145_P3_rcpt. IPR000493. InsP3_rcpt-bd. IPR005821. Ion_trans_dom. IPR016093. MIR_motif. IPR013662. RIH_assoc-dom. IPR015925. Ryanodine_recept-rel. [Graphical view]
PANTHER	PTHR13715. PTHR13715. 1 hit.
Pfam	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]
PRINTS	PR00779. INSP3RECEPTR.
SMART	SM00472. MIR. 4 hits. [Graphical view]
SUPFAM	SSF82109. MIR. 2 hits.
PROSITE	PS50919. MIR. 5 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q14571.
ChEMBL	CHEMBL2512.
ChiTaRS	ITPR2. human.
GenomeRNAi	3709.
NextBio	14539.
SOURCE	Search...

Entry information

Entry name

ITPR2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.