Q14573 (ITPR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol 1,4,5-trisphosphate receptor type 3

Alternative name(s):
IP3 receptor isoform 3
Short name=IP3R 3
Short name=InsP3R3
Type 3 inositol 1,4,5-trisphosphate receptor
Short name=Type 3 InsP3 receptor

Gene names

Name:

ITPR3

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	2671 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.
Subunit structure	Homotetramer. Interacts with SIGMAR1, PML, AKT1, TRPC1, TRPC3 and TRPC4 By similarity. Interacts with CABP1. Interacts with TMBIM4/LFG4. Ref.5 Ref.7
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Expressed in intestinal crypt and villus epithelial cells.
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	Phosphorylated on tyrosine residues. Phosphorylated by AKT1 on serine and/or threonine residues By similarity.
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	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	G-protein coupled receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL activation of phospholipase C activity Traceable author statement. Source: Reactome calcium ion transport into cytosol Inferred from sequence or structural similarity. Source: UniProtKB 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 protein heterooligomerization Inferred from sequence or structural similarity. Source: BHF-UCL protein homooligomerization Inferred from sequence or structural similarity. Source: BHF-UCL regulation of insulin secretion Traceable author statement. Source: Reactome response to calcium ion Inferred from direct assay PubMed 19052258. Source: BHF-UCL sensory perception of bitter taste Inferred from electronic annotation. Source: Compara sensory perception of sweet taste Inferred from electronic annotation. Source: Compara sensory perception of umami taste Inferred from electronic annotation. Source: Compara small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	apical part of cell Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL brush border Inferred from sequence or structural similarity Ref.2. Source: BHF-UCL endoplasmic reticulum membrane Inferred from direct assay PubMed 21062895. Source: UniProtKB integral to plasma membrane Inferred from direct assay PubMed 10828023. Source: BHF-UCL myelin sheath Inferred from sequence or structural similarity. Source: BHF-UCL neuronal cell body Inferred from sequence or structural similarity. Source: BHF-UCL nuclear outer membrane Inferred from sequence or structural similarity. Source: BHF-UCL nucleolus Inferred from electronic annotation. Source: Compara nucleoplasm Inferred from electronic annotation. Source: Compara platelet dense tubular network membrane Traceable author statement. Source: Reactome
Molecular_function	inositol 1,3,4,5 tetrakisphosphate binding Inferred from sequence or structural similarity. Source: BHF-UCL inositol 1,4,5 trisphosphate binding Inferred from direct assay Ref.2. Source: BHF-UCL inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Inferred from sequence or structural similarity. Source: UniProtKB inositol hexakisphosphate binding Inferred from sequence or structural similarity. Source: BHF-UCL intracellular ligand-gated calcium channel activity Inferred from sequence or structural similarity. Source: UniProtKB phosphatidylinositol binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRPC3	Q13507	5	EBI-351055,EBI-520807

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2671	2671	Inositol 1,4,5-trisphosphate receptor type 3		PRO_0000153928
Regions
	Topological domain	1 – 2202	2202	Cytoplasmic Potential
	Transmembrane	2203 – 2223	21	Helical; Potential
	Topological domain	2224 – 2235	12	Extracellular Potential
	Transmembrane	2236 – 2256	21	Helical; Potential
	Topological domain	2257 – 2264	8	Cytoplasmic Potential
	Transmembrane	2265 – 2285	21	Helical; Potential
	Topological domain	2286 – 2325	40	Extracellular Potential
	Transmembrane	2326 – 2346	21	Helical; Potential
	Topological domain	2347 – 2368	22	Cytoplasmic Potential
	Transmembrane	2369 – 2389	21	Helical; Potential
	Topological domain	2390 – 2496	107	Extracellular Potential
	Transmembrane	2497 – 2517	21	Helical; Potential
	Topological domain	2518 – 2671	154	Cytoplasmic Potential
	Domain	113 – 173	61	MIR 1
	Domain	174 – 224	51	MIR 2
	Domain	232 – 288	57	MIR 3
	Domain	295 – 372	78	MIR 4
	Domain	378 – 434	57	MIR 5
	Region	266 – 270	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	916	1	Phosphoserine Ref.6 Ref.9
	Modified residue	934	1	Phosphoserine Ref.6
	Modified residue	1813	1	Phosphoserine Ref.8
	Modified residue	1832	1	Phosphoserine Ref.6
	Modified residue	2583	1	Phosphotyrosine Potential
	Modified residue	2670	1	Phosphoserine Ref.9
Natural variations
	Natural variant	374	1	L → W. Corresponds to variant rs2229646 [ dbSNP | Ensembl ].		VAR_049604
	Natural variant	667	1	R → Q. Corresponds to variant rs11963294 [ dbSNP | Ensembl ].		VAR_046978
	Natural variant	742	1	D → E. Corresponds to variant rs2229633 [ dbSNP | Ensembl ].		VAR_046979
	Natural variant	1029	1	G → V. Corresponds to variant rs2296333 [ dbSNP | Ensembl ].		VAR_046980
	Natural variant	1552	1	L → V. Corresponds to variant rs9461899 [ dbSNP | Ensembl ].		VAR_046981
	Natural variant	1850	1	R → Q. Corresponds to variant rs12528378 [ dbSNP | Ensembl ].		VAR_046982
	Natural variant	2398	1	E → Q. Corresponds to variant rs2229641 [ dbSNP | Ensembl ].		VAR_046983
	Natural variant	2436	1	L → V. Ref.1 Corresponds to variant rs2229642 [ dbSNP | Ensembl ].		VAR_046984
Experimental info
	Sequence conflict	524	1	A → V in AAC50064. Ref.2
	Sequence conflict	562	1	H → Y in AAC50064. Ref.2
	Sequence conflict	989	1	Y → H in BAA05385. Ref.1
	Sequence conflict	1143	1	A → T in AAC50064. Ref.2
	Sequence conflict	1391	1	L → V in AAC50064. Ref.2
	Sequence conflict	1496 – 1497	2	TI → PV in AAC50064. Ref.2
	Sequence conflict	1674	1	L → V in AAC50064. Ref.2
	Sequence conflict	2187 – 2188	2	KL → NV in BAA05385. Ref.1
	Sequence conflict	2187 – 2188	2	KL → NV in AAC50064. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q14573 [UniParc]. Last modified October 14, 2008. Version 2. Checksum: 04D1957A53320EEE	FASTA	2,671	304,106
	10 20 30 40 50 60 MSEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK KFRDCLFKVC 70 80 90 100 110 120 PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME QKQNDTENKK VHGDVVKYGS 130 140 150 160 170 180 VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV TLDATGNEGS WLFIQPFWKL RSNGDNVVVG 190 200 210 220 230 240 DKVILNPVNA GQPLHASNYE LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV 250 260 270 280 290 300 VRLFHAEQEK FLTCDEYKGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW 310 320 330 340 350 360 NGLYRFKHLA TGNYLAAEEN PSYKGDASDP KAAGMGAQGR TGRRNAGEKI KYCLVAVPHG 370 380 390 400 410 420 NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS TNVPIDIEEE RPIRLMLGTC 430 440 450 460 470 480 PTKEDKEAFA IVSVPVSEIR DLDFANDASS MLASAVEKLN EGFISQNDRR FVIQLLEDLV 490 500 510 520 530 540 FFVSDVPNNG QNVLDIMVTK PNRERQKLMR EQNILKQVFG ILKAPFREKG GEGPLVRLEE 550 560 570 580 590 600 LSDQKNAPYQ HMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH 610 620 630 640 650 660 NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NHIAIPVTQE LICKCVLDPK 670 680 690 700 710 720 NSDILIRTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDKN NEHHEKSVRQ LAQEARAGNA 730 740 750 760 770 780 HDENVLSYYR YQLKLFARMC LDRQYLAIDE ISQQLGVDLI FLCMADEMLP FDLRASFCHL 790 800 810 820 830 840 MLHVHVDRDP QELVTPVKFA RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ANTMEFVEDY 850 860 870 880 890 900 LNNVVSEAVP FANEEKNKLT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCVQGPPA 910 920 930 940 950 960 MLQAYEDPGG KNVRRSIQGV GHMMSTMVLS RKQSVFSAPS LSAGASAAEP LDRSKFEENE 970 980 990 1000 1010 1020 DIVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE VFPMQDSGAD GTAPAFDSTT 1030 1040 1050 1060 1070 1080 ANMNLDRIGE QAEAMFGVGK TSSMLEVDDE GGRMFLRVLI HLTMHDYAPL VSGALQLLFK 1090 1100 1110 1120 1130 1140 HFSQRQEAMH TFKQVQLLIS AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSGKGEEVE 1150 1160 1170 1180 1190 1200 AGAAKDKKER PTDEEGFLHP PGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM 1210 1220 1230 1240 1250 1260 DAHKVMLDLL QIPYDKGDAK MMEILRYTHQ FLQKFCAGNP GNQALLHKHL HLFLTPGLLE 1270 1280 1290 1300 1310 1320 AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL DFLHTVIKAE GKYVKKCQDM 1330 1340 1350 1360 1370 1380 IMTELTNAGD DVVVFYNDKA SLAHLLDMMK AARDGVEDHS PLMYHISLVD LLAACAEGKN 1390 1400 1410 1420 1430 1440 VYTEIKCTSL LPLEDVVSVV THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL 1450 1460 1470 1480 1490 1500 FENFTLDMAR VCSKREKRVA DPTLEKYVLS VVLDTINAFF SSPFSENSTS LQTHQTIVVQ 1510 1520 1530 1540 1550 1560 LLQSTTRLLE CPWLQQQHKG SVEACIRTLA MVAKGRAILL PMDLDAHISS MLSSGASCAA 1570 1580 1590 1600 1610 1620 AAQRNASSYK ATTRAFPRVT PTANQWDYKN IIEKLQDIIT ALEERLKPLV QAELSVLVDV 1630 1640 1650 1660 1670 1680 LHWPELLFLE GSEAYQRCES GGFLSKLIQH TKDLMESEEK LCIKVLRTLQ QMLLKKTKYG 1690 1700 1710 1720 1730 1740 DRGNQLRKML LQNYLQNRKS TSRGDLPDPI GTGLDPDWSA IAATQCRLDK EGATKLVCDL 1750 1760 1770 1780 1790 1800 ITSTKNEKIF QESIGLAIHL LDGGNTEIQK SFHNLMMSDK KSERFFKVLH DRMKRAQQET 1810 1820 1830 1840 1850 1860 KSTVAVNMND LGSQPHEDRE PVDPTTKGRV ASFSIPGSSS RYSLGPSLRR GHEVSERVQS 1870 1880 1890 1900 1910 1920 SEMGTSVLIM QPILRFLQLL CENHNRDLQN FLRCQNNKTN YNLVCETLQF LDIMCGSTTG 1930 1940 1950 1960 1970 1980 GLGLLGLYIN EDNVGLVIQT LETLTEYCQG PCHENQTCIV THESNGIDII TALILNDISP 1990 2000 2010 2020 2030 2040 LCKYRMDLVL QLKDNASKLL LALMESRHDS ENAERILISL RPQELVDVIK KAYLQEEERE 2050 2060 2070 2080 2090 2100 NSEVSPREVG HNIYILALQL SRHNKQLQHL LKPVKRIQEE EAEGISSMLS LNNKQLSQML 2110 2120 2130 2140 2150 2160 KSSAPAQEEE EDPLAYYENH TSQIEIVRQD RSMEQIVFPV PGICQFLTEE TKHRLFTTTE 2170 2180 2190 2200 2210 2220 QDEQGSKVSD FFDQSSFLHN EMEWQRKLRS MPLIYWFSRR MTLWGSISFN LAVFINIIIA 2230 2240 2250 2260 2270 2280 FFYPYMEGAS TGVLDSPLIS LLFWILICFS IAALFTKRYS IRPLIVALIL RSIYYLGIGP 2290 2300 2310 2320 2330 2340 TLNILGALNL TNKIVFVVSF VGNRGTFIRG YKAMVMDMEF LYHVGYILTS VLGLFAHELF 2350 2360 2370 2380 2390 2400 YSILLFDLIY REETLFNVIK SVTRNGRSIL LTALLALILV YLFSIVGFLF LKDDFILEVD 2410 2420 2430 2440 2450 2460 RLPNNHSTAS PLGMPHGAAA FVDTCSGDKM DCVSGLSVPE VLEEDRELDS TERACDTLLM 2470 2480 2490 2500 2510 2520 CIVTVMNHGL RNGGGVGDIL RKPSKDESLF PARVVYDLLF FFIVIIIVLN LIFGVIIDTF 2530 2540 2550 2560 2570 2580 ADLRSEKQKK EEILKTTCFI CGLERDKFDN KTVSFEEHIK LEHNMWNYLY FIVLVRVKNK 2590 2600 2610 2620 2630 2640 TDYTGPESYV AQMIKNKNLD WFPRMRAMSL VSNEGEGEQN EIRILQDKLN STMKLVSHLT 2650 2660 2670 AQLNELKEQM TEQRKRRQRL GFVDVQNCIS R

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], VARIANT VAL-2436.
[2]	"Primary structure, ligand binding, and localization of the human type 3 inositol 1,4,5-trisphosphate receptor expressed in intestinal epithelium." Maranto A.R. J. Biol. Chem. 269:1222-1230(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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-916; SER-934 AND SER-1832, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Human Golgi antiapoptotic protein modulates intracellular calcium fluxes." de Mattia F., Gubser C., van Dommelen M.M., Visch H.J., Distelmaier F., Postigo A., Luyten T., Parys J.B., de Smedt H., Smith G.L., Willems P.H., van Kuppeveld F.J. Mol. Biol. Cell 20:3638-3645(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TMBIM4/LFG4.
[8]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1813, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916 AND SER-2670, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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	D26351 mRNA. Translation: BAA05385.1. U01062 mRNA. Translation: AAC50064.1. AL139044 Genomic DNA. Translation: CAI16455.1. CH471081 Genomic DNA. Translation: EAX03744.1.
IPI	IPI00291607.
PIR	A49873.
RefSeq	NP_002215.2. NM_002224.3.
UniGene	Hs.65758.
3D structure databases
ProteinModelPortal	Q14573.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14573. 8 interactions.
STRING	9606.ENSP00000363435.
PTM databases
PhosphoSite	Q14573.
Polymorphism databases
DMDM	209572633.
Proteomic databases
PaxDb	Q14573.
PeptideAtlas	Q14573.
PRIDE	Q14573.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374316; ENSP00000363435; ENSG00000096433.
GeneID	3710.
KEGG	hsa:3710.
UCSC	uc021ywr.1. human.
Organism-specific databases
CTD	3710.
GeneCards	GC06P033588.
H-InvDB	HIX0005781.
HGNC	HGNC:6182. ITPR3.
HPA	HPA003915.
MIM	147267. gene.
neXtProt	NX_Q14573.
PharmGKB	PA29980.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG280601.
HOGENOM	HOG000007660.
HOVERGEN	HBG052158.
InParanoid	Q14573.
KO	K04960.
OMA	LRASFCH.
OrthoDB	EOG4GQQ42.
PhylomeDB	Q14573.
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	Q14573.
Bgee	Q14573.
CleanEx	HS_ITPR3.
Genevestigator	Q14573.
GermOnline	ENSG00000096433. 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	Q14573.
ChEMBL	CHEMBL3904.
ChiTaRS	ITPR3. human.
GenomeRNAi	3710.
NextBio	14543.
SOURCE	Search...

Entry information

Entry name

ITPR3_HUMAN

Accession

Primary (citable) accession number: Q14573
Secondary accession number(s): Q14649, Q5TAQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	October 14, 2008
Last modified:	May 1, 2013
This is version 132 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.