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Q14573

- ITPR3_HUMAN

UniProt

Q14573 - ITPR3_HUMAN

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Protein
Inositol 1,4,5-trisphosphate receptor type 3
Gene
ITPR3
Organism
Homo sapiens (Human)
Status
Reviewed - 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
  7. protein binding Source: UniProtKB

GO - Biological processi

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

Organism-specific databases

HGNCiHGNC:6182. ITPR3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22022202Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2203 – 222321Helical; Reviewed prediction
Add
BLAST
Topological domaini2224 – 223512Extracellular Reviewed prediction
Add
BLAST
Transmembranei2236 – 225621Helical; Reviewed prediction
Add
BLAST
Topological domaini2257 – 22648Cytoplasmic Reviewed prediction
Transmembranei2265 – 228521Helical; Reviewed prediction
Add
BLAST
Topological domaini2286 – 232540Extracellular Reviewed prediction
Add
BLAST
Transmembranei2326 – 234621Helical; Reviewed prediction
Add
BLAST
Topological domaini2347 – 236822Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei2369 – 238921Helical; Reviewed prediction
Add
BLAST
Topological domaini2390 – 2496107Extracellular Reviewed prediction
Add
BLAST
Transmembranei2497 – 251721Helical; Reviewed prediction
Add
BLAST
Topological domaini2518 – 2671154Cytoplasmic Reviewed prediction
Add
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. myelin sheath Source: BHF-UCL
  8. neuronal cell body Source: BHF-UCL
  9. nuclear outer membrane Source: BHF-UCL
  10. nucleolus Source: Ensembl
  11. nucleoplasm Source: Ensembl
  12. plasma membrane Source: UniProtKB
  13. platelet dense tubular network membrane Source: Reactome
  14. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29980.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 26712671Inositol 1,4,5-trisphosphate receptor type 3
PRO_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 – 18321Phosphoserine1 Publication
Modified residuei2583 – 25831Phosphotyrosine Reviewed prediction
Modified residuei2670 – 26701Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues. Phosphorylated by AKT1 on serine and/or threonine residues 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

ArrayExpressiQ14573.
BgeeiQ14573.
CleanExiHS_ITPR3.
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.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109915. 17 interactions.
IntActiQ14573. 9 interactions.
MINTiMINT-4991384.
STRINGi9606.ENSP00000363435.

Structurei

3D structure databases

ProteinModelPortaliQ14573.
SMRiQ14573. Positions 4-579.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni266 – 2705Inositol 1,4,5-trisphosphate binding By similarity
Regioni507 – 5104Inositol 1,4,5-trisphosphate binding By similarity
Regioni567 – 5693Inositol 1,4,5-trisphosphate binding By 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.
Contains 5 MIR domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG280601.
HOGENOMiHOG000007660.
HOVERGENiHBG052158.
InParanoidiQ14573.
KOiK04960.
OMAiKGDAKMM.
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

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MSEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK     50
KFRDCLFKVC PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME 100
QKQNDTENKK VHGDVVKYGS VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV 150
TLDATGNEGS WLFIQPFWKL RSNGDNVVVG DKVILNPVNA GQPLHASNYE 200
LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV VRLFHAEQEK 250
FLTCDEYKGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW 300
NGLYRFKHLA TGNYLAAEEN PSYKGDASDP KAAGMGAQGR TGRRNAGEKI 350
KYCLVAVPHG NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS 400
TNVPIDIEEE RPIRLMLGTC PTKEDKEAFA IVSVPVSEIR DLDFANDASS 450
MLASAVEKLN EGFISQNDRR FVIQLLEDLV FFVSDVPNNG QNVLDIMVTK 500
PNRERQKLMR EQNILKQVFG ILKAPFREKG GEGPLVRLEE LSDQKNAPYQ 550
HMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH 600
NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NHIAIPVTQE 650
LICKCVLDPK NSDILIRTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDKN 700
NEHHEKSVRQ LAQEARAGNA HDENVLSYYR YQLKLFARMC LDRQYLAIDE 750
ISQQLGVDLI FLCMADEMLP FDLRASFCHL MLHVHVDRDP QELVTPVKFA 800
RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ANTMEFVEDY LNNVVSEAVP 850
FANEEKNKLT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCVQGPPA 900
MLQAYEDPGG KNVRRSIQGV GHMMSTMVLS RKQSVFSAPS LSAGASAAEP 950
LDRSKFEENE DIVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE 1000
VFPMQDSGAD GTAPAFDSTT ANMNLDRIGE QAEAMFGVGK TSSMLEVDDE 1050
GGRMFLRVLI HLTMHDYAPL VSGALQLLFK HFSQRQEAMH TFKQVQLLIS 1100
AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSGKGEEVE AGAAKDKKER 1150
PTDEEGFLHP PGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM 1200
DAHKVMLDLL QIPYDKGDAK MMEILRYTHQ FLQKFCAGNP GNQALLHKHL 1250
HLFLTPGLLE AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL 1300
DFLHTVIKAE GKYVKKCQDM IMTELTNAGD DVVVFYNDKA SLAHLLDMMK 1350
AARDGVEDHS PLMYHISLVD LLAACAEGKN VYTEIKCTSL LPLEDVVSVV 1400
THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL FENFTLDMAR 1450
VCSKREKRVA DPTLEKYVLS VVLDTINAFF SSPFSENSTS LQTHQTIVVQ 1500
LLQSTTRLLE CPWLQQQHKG SVEACIRTLA MVAKGRAILL PMDLDAHISS 1550
MLSSGASCAA AAQRNASSYK ATTRAFPRVT PTANQWDYKN IIEKLQDIIT 1600
ALEERLKPLV QAELSVLVDV LHWPELLFLE GSEAYQRCES GGFLSKLIQH 1650
TKDLMESEEK LCIKVLRTLQ QMLLKKTKYG DRGNQLRKML LQNYLQNRKS 1700
TSRGDLPDPI GTGLDPDWSA IAATQCRLDK EGATKLVCDL ITSTKNEKIF 1750
QESIGLAIHL LDGGNTEIQK SFHNLMMSDK KSERFFKVLH DRMKRAQQET 1800
KSTVAVNMND LGSQPHEDRE PVDPTTKGRV ASFSIPGSSS RYSLGPSLRR 1850
GHEVSERVQS SEMGTSVLIM QPILRFLQLL CENHNRDLQN FLRCQNNKTN 1900
YNLVCETLQF LDIMCGSTTG GLGLLGLYIN EDNVGLVIQT LETLTEYCQG 1950
PCHENQTCIV THESNGIDII TALILNDISP LCKYRMDLVL QLKDNASKLL 2000
LALMESRHDS ENAERILISL RPQELVDVIK KAYLQEEERE NSEVSPREVG 2050
HNIYILALQL SRHNKQLQHL LKPVKRIQEE EAEGISSMLS LNNKQLSQML 2100
KSSAPAQEEE EDPLAYYENH TSQIEIVRQD RSMEQIVFPV PGICQFLTEE 2150
TKHRLFTTTE QDEQGSKVSD FFDQSSFLHN EMEWQRKLRS MPLIYWFSRR 2200
MTLWGSISFN LAVFINIIIA FFYPYMEGAS TGVLDSPLIS LLFWILICFS 2250
IAALFTKRYS IRPLIVALIL RSIYYLGIGP TLNILGALNL TNKIVFVVSF 2300
VGNRGTFIRG YKAMVMDMEF LYHVGYILTS VLGLFAHELF YSILLFDLIY 2350
REETLFNVIK SVTRNGRSIL LTALLALILV YLFSIVGFLF LKDDFILEVD 2400
RLPNNHSTAS PLGMPHGAAA FVDTCSGDKM DCVSGLSVPE VLEEDRELDS 2450
TERACDTLLM CIVTVMNHGL RNGGGVGDIL RKPSKDESLF PARVVYDLLF 2500
FFIVIIIVLN LIFGVIIDTF ADLRSEKQKK EEILKTTCFI CGLERDKFDN 2550
KTVSFEEHIK LEHNMWNYLY FIVLVRVKNK TDYTGPESYV AQMIKNKNLD 2600
WFPRMRAMSL VSNEGEGEQN EIRILQDKLN STMKLVSHLT AQLNELKEQM 2650
TEQRKRRQRL GFVDVQNCIS R 2671
Length:2,671
Mass (Da):304,106
Last modified:October 14, 2008 - v2
Checksum:i04D1957A53320EEE
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti524 – 5241A → V in AAC50064. 1 Publication
Sequence conflicti562 – 5621H → Y in AAC50064. 1 Publication
Sequence conflicti989 – 9891Y → H in BAA05385. 1 Publication
Sequence conflicti1143 – 11431A → T in AAC50064. 1 Publication
Sequence conflicti1391 – 13911L → V in AAC50064. 1 Publication
Sequence conflicti1496 – 14972TI → PV in AAC50064. 1 Publication
Sequence conflicti1674 – 16741L → V in AAC50064. 1 Publication
Sequence conflicti2187 – 21882KL → NV in BAA05385. 1 Publication
Sequence conflicti2187 – 21882KL → NV in AAC50064. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 databases

DMDMi209572633.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D26351 mRNA. Translation: BAA05385.1 .
U01062 mRNA. Translation: AAC50064.1 .
AL139044 Genomic DNA. Translation: CAI16455.1 .
CH471081 Genomic DNA. Translation: EAX03744.1 .
CCDSi CCDS4783.1.
PIRi A49873.
RefSeqi NP_002215.2. NM_002224.3.
UniGenei Hs.65758.

3D structure databases

ProteinModelPortali Q14573.
SMRi Q14573. Positions 4-579.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109915. 17 interactions.
IntActi Q14573. 9 interactions.
MINTi MINT-4991384.
STRINGi 9606.ENSP00000363435.

Chemistry

BindingDBi Q14573.
ChEMBLi CHEMBL2111451.
GuidetoPHARMACOLOGYi 745.

PTM databases

PhosphoSitei Q14573.

Polymorphism databases

DMDMi 209572633.

Proteomic databases

MaxQBi Q14573.
PaxDbi Q14573.
PeptideAtlasi Q14573.
PRIDEi Q14573.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374316 ; ENSP00000363435 ; ENSG00000096433 .
ENST00000605930 ; ENSP00000475177 ; ENSG00000096433 .
GeneIDi 3710.
KEGGi hsa:3710.
UCSCi uc021ywr.1. human.

Organism-specific databases

CTDi 3710.
GeneCardsi GC06P033588.
H-InvDB HIX0005781.
HGNCi HGNC:6182. ITPR3.
HPAi HPA003915.
MIMi 147267. gene.
neXtProti NX_Q14573.
PharmGKBi PA29980.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG280601.
HOGENOMi HOG000007660.
HOVERGENi HBG052158.
InParanoidi Q14573.
KOi K04960.
OMAi KGDAKMM.
OrthoDBi EOG76HQ0M.
PhylomeDBi Q14573.
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 ITPR3. human.
GeneWikii ITPR3.
GenomeRNAii 3710.
NextBioi 14543.
PROi Q14573.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q14573.
Bgeei Q14573.
CleanExi HS_ITPR3.
Genevestigatori Q14573.

Family and domain databases

Gene3Di 1.25.10.30. 2 hits.
InterProi 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.
SSF82109. SSF82109. 2 hits.
PROSITEi PS50919. MIR. 5 hits.
[Graphical view ]
ProtoNeti Search...

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.

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: September 3, 2014
This is version 146 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

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