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Protein

Inositol 1,4,5-trisphosphate receptor type 3

Gene

ITPR3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for inositol 1,4,5-trisphosphate, a second messenger that mediates the release of intracellular calcium.

GO - Molecular functioni

  1. inositol 1,3,4,5 tetrakisphosphate binding Source: BHF-UCL
  2. inositol 1,4,5 trisphosphate binding Source: BHF-UCL
  3. inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity Source: UniProtKB
  4. inositol hexakisphosphate binding Source: BHF-UCL
  5. intracellular ligand-gated calcium channel activity Source: UniProtKB
  6. phosphatidylinositol binding Source: Ensembl

GO - Biological processi

  1. activation of phospholipase C activity Source: Reactome
  2. blood coagulation Source: Reactome
  3. calcium ion transport into cytosol Source: UniProtKB
  4. energy reserve metabolic process Source: Reactome
  5. epidermal growth factor receptor signaling pathway Source: Reactome
  6. Fc-epsilon receptor signaling pathway Source: Reactome
  7. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  8. fibroblast growth factor receptor signaling pathway Source: Reactome
  9. G-protein coupled receptor signaling pathway Source: BHF-UCL
  10. innate immune response Source: Reactome
  11. inositol phosphate-mediated signaling Source: GOC
  12. long-term synaptic potentiation Source: Ensembl
  13. memory Source: Ensembl
  14. neurotrophin TRK receptor signaling pathway Source: Reactome
  15. platelet activation Source: Reactome
  16. positive regulation of cytosolic calcium ion concentration Source: BHF-UCL
  17. protein heterooligomerization Source: BHF-UCL
  18. protein homooligomerization Source: BHF-UCL
  19. regulation of insulin secretion Source: Reactome
  20. response to calcium ion Source: BHF-UCL
  21. sensory perception of bitter taste Source: Ensembl
  22. sensory perception of sweet taste Source: Ensembl
  23. sensory perception of umami taste Source: Ensembl
  24. signal transduction Source: Reactome
  25. small molecule metabolic process Source: Reactome
  26. vascular endothelial growth factor receptor signaling pathway Source: Reactome
Complete GO annotation...

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_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18325. Regulation of insulin secretion.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_263982. Ca2+ pathway.
REACT_264273. VEGFR2 mediated cell proliferation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ITPR3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6182. ITPR3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22022202CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei2203 – 222321HelicalSequence AnalysisAdd
BLAST
Topological domaini2224 – 223512ExtracellularSequence AnalysisAdd
BLAST
Transmembranei2236 – 225621HelicalSequence AnalysisAdd
BLAST
Topological domaini2257 – 22648CytoplasmicSequence Analysis
Transmembranei2265 – 228521HelicalSequence AnalysisAdd
BLAST
Topological domaini2286 – 232540ExtracellularSequence AnalysisAdd
BLAST
Transmembranei2326 – 234621HelicalSequence AnalysisAdd
BLAST
Topological domaini2347 – 236822CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei2369 – 238921HelicalSequence AnalysisAdd
BLAST
Topological domaini2390 – 2496107ExtracellularSequence AnalysisAdd
BLAST
Transmembranei2497 – 251721HelicalSequence AnalysisAdd
BLAST
Topological domaini2518 – 2671154CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. apical part of cell Source: BHF-UCL
  2. brush border Source: BHF-UCL
  3. cytoplasm Source: BHF-UCL
  4. endoplasmic reticulum Source: BHF-UCL
  5. endoplasmic reticulum membrane Source: UniProtKB
  6. integral component of plasma membrane Source: BHF-UCL
  7. membrane Source: UniProtKB
  8. myelin sheath Source: BHF-UCL
  9. neuronal cell body Source: BHF-UCL
  10. nuclear outer membrane Source: BHF-UCL
  11. nucleolus Source: Ensembl
  12. nucleoplasm Source: Ensembl
  13. plasma membrane Source: UniProtKB
  14. platelet dense tubular network membrane Source: Reactome
  15. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29980.

Chemistry

DrugBankiDB00201. Caffeine.

Polymorphism and mutation databases

BioMutaiITPR3.
DMDMi209572633.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26712671Inositol 1,4,5-trisphosphate receptor type 3PRO_0000153928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei916 – 9161Phosphoserine2 Publications
Modified residuei934 – 9341Phosphoserine1 Publication
Modified residuei1813 – 18131Phosphoserine1 Publication
Modified residuei1832 – 18321Phosphoserine2 Publications
Modified residuei2583 – 25831PhosphotyrosineSequence Analysis
Modified residuei2670 – 26701Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues. Phosphorylated by AKT1 on serine and/or threonine residues (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ14573.
PaxDbiQ14573.
PeptideAtlasiQ14573.
PRIDEiQ14573.

PTM databases

PhosphoSiteiQ14573.

Expressioni

Tissue specificityi

Expressed in intestinal crypt and villus epithelial cells.

Gene expression databases

BgeeiQ14573.
CleanExiHS_ITPR3.
ExpressionAtlasiQ14573. baseline and differential.
GenevestigatoriQ14573.

Organism-specific databases

HPAiHPA003915.

Interactioni

Subunit structurei

Homotetramer. Interacts with SIGMAR1, PML, AKT1, TRPC1, TRPC3 and TRPC4 (By similarity). Interacts with LRMP (via coiled-coil domain) (By similarity). Interacts with CABP1. Interacts with TMBIM4/LFG4. Interacts with CEMIP. Interacts with TESPA1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
TRPC3Q135075EBI-351055,EBI-520807

Protein-protein interaction databases

BioGridi109915. 24 interactions.
IntActiQ14573. 9 interactions.
MINTiMINT-4991384.
STRINGi9606.ENSP00000363435.

Structurei

3D structure databases

ProteinModelPortaliQ14573.
SMRiQ14573. Positions 4-579.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini113 – 17361MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini174 – 22451MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini232 – 28857MIR 3PROSITE-ProRule annotationAdd
BLAST
Domaini295 – 37278MIR 4PROSITE-ProRule annotationAdd
BLAST
Domaini378 – 43457MIR 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni266 – 2705Inositol 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.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiQ14573.
KOiK04960.
OMAiFVHELFY.
OrthoDBiEOG76HQ0M.
PhylomeDBiQ14573.
TreeFamiTF312815.

Family and domain databases

Gene3Di1.25.10.30. 2 hits.
InterProiIPR014821. 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.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50919. MIR. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q14573-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK
60 70 80 90 100
KFRDCLFKVC PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME
110 120 130 140 150
QKQNDTENKK VHGDVVKYGS VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV
160 170 180 190 200
TLDATGNEGS WLFIQPFWKL RSNGDNVVVG DKVILNPVNA GQPLHASNYE
210 220 230 240 250
LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV VRLFHAEQEK
260 270 280 290 300
FLTCDEYKGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW
310 320 330 340 350
NGLYRFKHLA TGNYLAAEEN PSYKGDASDP KAAGMGAQGR TGRRNAGEKI
360 370 380 390 400
KYCLVAVPHG NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS
410 420 430 440 450
TNVPIDIEEE RPIRLMLGTC PTKEDKEAFA IVSVPVSEIR DLDFANDASS
460 470 480 490 500
MLASAVEKLN EGFISQNDRR FVIQLLEDLV FFVSDVPNNG QNVLDIMVTK
510 520 530 540 550
PNRERQKLMR EQNILKQVFG ILKAPFREKG GEGPLVRLEE LSDQKNAPYQ
560 570 580 590 600
HMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
610 620 630 640 650
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NHIAIPVTQE
660 670 680 690 700
LICKCVLDPK NSDILIRTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDKN
710 720 730 740 750
NEHHEKSVRQ LAQEARAGNA HDENVLSYYR YQLKLFARMC LDRQYLAIDE
760 770 780 790 800
ISQQLGVDLI FLCMADEMLP FDLRASFCHL MLHVHVDRDP QELVTPVKFA
810 820 830 840 850
RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ANTMEFVEDY LNNVVSEAVP
860 870 880 890 900
FANEEKNKLT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCVQGPPA
910 920 930 940 950
MLQAYEDPGG KNVRRSIQGV GHMMSTMVLS RKQSVFSAPS LSAGASAAEP
960 970 980 990 1000
LDRSKFEENE DIVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE
1010 1020 1030 1040 1050
VFPMQDSGAD GTAPAFDSTT ANMNLDRIGE QAEAMFGVGK TSSMLEVDDE
1060 1070 1080 1090 1100
GGRMFLRVLI HLTMHDYAPL VSGALQLLFK HFSQRQEAMH TFKQVQLLIS
1110 1120 1130 1140 1150
AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSGKGEEVE AGAAKDKKER
1160 1170 1180 1190 1200
PTDEEGFLHP PGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM
1210 1220 1230 1240 1250
DAHKVMLDLL QIPYDKGDAK MMEILRYTHQ FLQKFCAGNP GNQALLHKHL
1260 1270 1280 1290 1300
HLFLTPGLLE AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL
1310 1320 1330 1340 1350
DFLHTVIKAE GKYVKKCQDM IMTELTNAGD DVVVFYNDKA SLAHLLDMMK
1360 1370 1380 1390 1400
AARDGVEDHS PLMYHISLVD LLAACAEGKN VYTEIKCTSL LPLEDVVSVV
1410 1420 1430 1440 1450
THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL FENFTLDMAR
1460 1470 1480 1490 1500
VCSKREKRVA DPTLEKYVLS VVLDTINAFF SSPFSENSTS LQTHQTIVVQ
1510 1520 1530 1540 1550
LLQSTTRLLE CPWLQQQHKG SVEACIRTLA MVAKGRAILL PMDLDAHISS
1560 1570 1580 1590 1600
MLSSGASCAA AAQRNASSYK ATTRAFPRVT PTANQWDYKN IIEKLQDIIT
1610 1620 1630 1640 1650
ALEERLKPLV QAELSVLVDV LHWPELLFLE GSEAYQRCES GGFLSKLIQH
1660 1670 1680 1690 1700
TKDLMESEEK LCIKVLRTLQ QMLLKKTKYG DRGNQLRKML LQNYLQNRKS
1710 1720 1730 1740 1750
TSRGDLPDPI GTGLDPDWSA IAATQCRLDK EGATKLVCDL ITSTKNEKIF
1760 1770 1780 1790 1800
QESIGLAIHL LDGGNTEIQK SFHNLMMSDK KSERFFKVLH DRMKRAQQET
1810 1820 1830 1840 1850
KSTVAVNMND LGSQPHEDRE PVDPTTKGRV ASFSIPGSSS RYSLGPSLRR
1860 1870 1880 1890 1900
GHEVSERVQS SEMGTSVLIM QPILRFLQLL CENHNRDLQN FLRCQNNKTN
1910 1920 1930 1940 1950
YNLVCETLQF LDIMCGSTTG GLGLLGLYIN EDNVGLVIQT LETLTEYCQG
1960 1970 1980 1990 2000
PCHENQTCIV THESNGIDII TALILNDISP LCKYRMDLVL QLKDNASKLL
2010 2020 2030 2040 2050
LALMESRHDS ENAERILISL RPQELVDVIK KAYLQEEERE NSEVSPREVG
2060 2070 2080 2090 2100
HNIYILALQL SRHNKQLQHL LKPVKRIQEE EAEGISSMLS LNNKQLSQML
2110 2120 2130 2140 2150
KSSAPAQEEE EDPLAYYENH TSQIEIVRQD RSMEQIVFPV PGICQFLTEE
2160 2170 2180 2190 2200
TKHRLFTTTE QDEQGSKVSD FFDQSSFLHN EMEWQRKLRS MPLIYWFSRR
2210 2220 2230 2240 2250
MTLWGSISFN LAVFINIIIA FFYPYMEGAS TGVLDSPLIS LLFWILICFS
2260 2270 2280 2290 2300
IAALFTKRYS IRPLIVALIL RSIYYLGIGP TLNILGALNL TNKIVFVVSF
2310 2320 2330 2340 2350
VGNRGTFIRG YKAMVMDMEF LYHVGYILTS VLGLFAHELF YSILLFDLIY
2360 2370 2380 2390 2400
REETLFNVIK SVTRNGRSIL LTALLALILV YLFSIVGFLF LKDDFILEVD
2410 2420 2430 2440 2450
RLPNNHSTAS PLGMPHGAAA FVDTCSGDKM DCVSGLSVPE VLEEDRELDS
2460 2470 2480 2490 2500
TERACDTLLM CIVTVMNHGL RNGGGVGDIL RKPSKDESLF PARVVYDLLF
2510 2520 2530 2540 2550
FFIVIIIVLN LIFGVIIDTF ADLRSEKQKK EEILKTTCFI CGLERDKFDN
2560 2570 2580 2590 2600
KTVSFEEHIK LEHNMWNYLY FIVLVRVKNK TDYTGPESYV AQMIKNKNLD
2610 2620 2630 2640 2650
WFPRMRAMSL VSNEGEGEQN EIRILQDKLN STMKLVSHLT AQLNELKEQM
2660 2670
TEQRKRRQRL GFVDVQNCIS R
Length:2,671
Mass (Da):304,106
Last modified:October 14, 2008 - v2
Checksum:i04D1957A53320EEE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti524 – 5241A → V in AAC50064 (PubMed:8288584).Curated
Sequence conflicti562 – 5621H → Y in AAC50064 (PubMed:8288584).Curated
Sequence conflicti989 – 9891Y → H in BAA05385 (PubMed:8081734).Curated
Sequence conflicti1143 – 11431A → T in AAC50064 (PubMed:8288584).Curated
Sequence conflicti1391 – 13911L → V in AAC50064 (PubMed:8288584).Curated
Sequence conflicti1496 – 14972TI → PV in AAC50064 (PubMed:8288584).Curated
Sequence conflicti1674 – 16741L → V in AAC50064 (PubMed:8288584).Curated
Sequence conflicti2187 – 21882KL → NV in BAA05385 (PubMed:8081734).Curated
Sequence conflicti2187 – 21882KL → NV in AAC50064 (PubMed:8288584).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti374 – 3741L → W.
Corresponds to variant rs2229646 [ dbSNP | Ensembl ].
VAR_049604
Natural varianti667 – 6671R → Q.
Corresponds to variant rs11963294 [ dbSNP | Ensembl ].
VAR_046978
Natural varianti742 – 7421D → E.
Corresponds to variant rs2229633 [ dbSNP | Ensembl ].
VAR_046979
Natural varianti1029 – 10291G → V.
Corresponds to variant rs2296333 [ dbSNP | Ensembl ].
VAR_046980
Natural varianti1552 – 15521L → V.
Corresponds to variant rs9461899 [ dbSNP | Ensembl ].
VAR_046981
Natural varianti1850 – 18501R → Q.
Corresponds to variant rs12528378 [ dbSNP | Ensembl ].
VAR_046982
Natural varianti2398 – 23981E → Q.
Corresponds to variant rs2229641 [ dbSNP | Ensembl ].
VAR_046983
Natural varianti2436 – 24361L → V.1 Publication
Corresponds to variant rs2229642 [ dbSNP | Ensembl ].
VAR_046984

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26351 mRNA. Translation: BAA05385.1.
U01062 mRNA. Translation: AAC50064.1.
AL139044 Genomic DNA. Translation: CAI16455.1.
CH471081 Genomic DNA. Translation: EAX03744.1.
CCDSiCCDS4783.1.
PIRiA49873.
RefSeqiNP_002215.2. NM_002224.3.
UniGeneiHs.65758.

Genome annotation databases

EnsembliENST00000374316; ENSP00000363435; ENSG00000096433.
ENST00000605930; ENSP00000475177; ENSG00000096433.
GeneIDi3710.
KEGGihsa:3710.
UCSCiuc021ywr.1. human.

Polymorphism and mutation databases

BioMutaiITPR3.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26351 mRNA. Translation: BAA05385.1.
U01062 mRNA. Translation: AAC50064.1.
AL139044 Genomic DNA. Translation: CAI16455.1.
CH471081 Genomic DNA. Translation: EAX03744.1.
CCDSiCCDS4783.1.
PIRiA49873.
RefSeqiNP_002215.2. NM_002224.3.
UniGeneiHs.65758.

3D structure databases

ProteinModelPortaliQ14573.
SMRiQ14573. Positions 4-579.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109915. 24 interactions.
IntActiQ14573. 9 interactions.
MINTiMINT-4991384.
STRINGi9606.ENSP00000363435.

Chemistry

BindingDBiQ14573.
ChEMBLiCHEMBL3904.
DrugBankiDB00201. Caffeine.
GuidetoPHARMACOLOGYi745.

PTM databases

PhosphoSiteiQ14573.

Polymorphism and mutation databases

BioMutaiITPR3.
DMDMi209572633.

Proteomic databases

MaxQBiQ14573.
PaxDbiQ14573.
PeptideAtlasiQ14573.
PRIDEiQ14573.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374316; ENSP00000363435; ENSG00000096433.
ENST00000605930; ENSP00000475177; ENSG00000096433.
GeneIDi3710.
KEGGihsa:3710.
UCSCiuc021ywr.1. human.

Organism-specific databases

CTDi3710.
GeneCardsiGC06P033588.
H-InvDBHIX0005781.
HGNCiHGNC:6182. ITPR3.
HPAiHPA003915.
MIMi147267. gene.
neXtProtiNX_Q14573.
PharmGKBiPA29980.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG280601.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiQ14573.
KOiK04960.
OMAiFVHELFY.
OrthoDBiEOG76HQ0M.
PhylomeDBiQ14573.
TreeFamiTF312815.

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_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
REACT_18325. Regulation of insulin secretion.
REACT_2202. Effects of PIP2 hydrolysis.
REACT_263982. Ca2+ pathway.
REACT_264273. VEGFR2 mediated cell proliferation.

Miscellaneous databases

ChiTaRSiITPR3. human.
GeneWikiiITPR3.
GenomeRNAii3710.
NextBioi14543.
PROiQ14573.
SOURCEiSearch...

Gene expression databases

BgeeiQ14573.
CleanExiHS_ITPR3.
ExpressionAtlasiQ14573. baseline and differential.
GenevestigatoriQ14573.

Family and domain databases

Gene3Di1.25.10.30. 2 hits.
InterProiIPR014821. 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.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-916; SER-934 AND SER-1832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Early insights into the function of KIAA1199, a markedly overexpressed protein in human colorectal tumors."
    Tiwari A., Schneider M., Fiorino A., Haider R., Okoniewski M.J., Roschitzki B., Uzozie A., Menigatti M., Jiricny J., Marra G.
    PLoS ONE 8:E69473-E69473(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CEMIP.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiITPR3_HUMAN
AccessioniPrimary (citable) accession number: Q14573
Secondary accession number(s): Q14649, Q5TAQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: October 14, 2008
Last modified: April 29, 2015
This is version 153 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.