Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q14573 (ITPR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2671 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.

Subunit structure

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. Ref.5 Ref.7 Ref.11

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 processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   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

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

blood coagulation

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

innate immune response

Traceable author statement. Source: Reactome

long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

memory

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of cytosolic calcium ion concentration

Inferred from sequence or structural similarity. Source: BHF-UCL

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: Ensembl

sensory perception of sweet taste

Inferred from electronic annotation. Source: Ensembl

sensory perception of umami taste

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentapical 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

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: BHF-UCL

endoplasmic reticulum membrane

Inferred from direct assay PubMed 21062895. Source: UniProtKB

integral component of 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: Ensembl

nucleoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 21062895. Source: UniProtKB

platelet dense tubular network membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functioninositol 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: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRPC3Q135075EBI-351055,EBI-520807

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26712671Inositol 1,4,5-trisphosphate receptor type 3
PRO_0000153928

Regions

Topological domain1 – 22022202Cytoplasmic Potential
Transmembrane2203 – 222321Helical; Potential
Topological domain2224 – 223512Extracellular Potential
Transmembrane2236 – 225621Helical; Potential
Topological domain2257 – 22648Cytoplasmic Potential
Transmembrane2265 – 228521Helical; Potential
Topological domain2286 – 232540Extracellular Potential
Transmembrane2326 – 234621Helical; Potential
Topological domain2347 – 236822Cytoplasmic Potential
Transmembrane2369 – 238921Helical; Potential
Topological domain2390 – 2496107Extracellular Potential
Transmembrane2497 – 251721Helical; Potential
Topological domain2518 – 2671154Cytoplasmic Potential
Domain113 – 17361MIR 1
Domain174 – 22451MIR 2
Domain232 – 28857MIR 3
Domain295 – 37278MIR 4
Domain378 – 43457MIR 5
Region266 – 2705Inositol 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 residue9161Phosphoserine Ref.6 Ref.9
Modified residue9341Phosphoserine Ref.6
Modified residue18131Phosphoserine Ref.8
Modified residue18321Phosphoserine Ref.6
Modified residue25831Phosphotyrosine Potential
Modified residue26701Phosphoserine Ref.9

Natural variations

Natural variant3741L → W.
Corresponds to variant rs2229646 [ dbSNP | Ensembl ].
VAR_049604
Natural variant6671R → Q.
Corresponds to variant rs11963294 [ dbSNP | Ensembl ].
VAR_046978
Natural variant7421D → E.
Corresponds to variant rs2229633 [ dbSNP | Ensembl ].
VAR_046979
Natural variant10291G → V.
Corresponds to variant rs2296333 [ dbSNP | Ensembl ].
VAR_046980
Natural variant15521L → V.
Corresponds to variant rs9461899 [ dbSNP | Ensembl ].
VAR_046981
Natural variant18501R → Q.
Corresponds to variant rs12528378 [ dbSNP | Ensembl ].
VAR_046982
Natural variant23981E → Q.
Corresponds to variant rs2229641 [ dbSNP | Ensembl ].
VAR_046983
Natural variant24361L → V. Ref.1
Corresponds to variant rs2229642 [ dbSNP | Ensembl ].
VAR_046984

Experimental info

Sequence conflict5241A → V in AAC50064. Ref.2
Sequence conflict5621H → Y in AAC50064. Ref.2
Sequence conflict9891Y → H in BAA05385. Ref.1
Sequence conflict11431A → T in AAC50064. Ref.2
Sequence conflict13911L → V in AAC50064. Ref.2
Sequence conflict1496 – 14972TI → PV in AAC50064. Ref.2
Sequence conflict16741L → V in AAC50064. Ref.2
Sequence conflict2187 – 21882KL → NV in BAA05385. Ref.1
Sequence conflict2187 – 21882KL → NV in AAC50064. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q14573 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 04D1957A53320EEE

FASTA2,671304,106
        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 

« Hide

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], 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, 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]"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].
[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.
+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.
PIRA49873.
RefSeqNP_002215.2. NM_002224.3.
UniGeneHs.65758.

3D structure databases

ProteinModelPortalQ14573.
SMRQ14573. Positions 4-579, 1188-1251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109915. 17 interactions.
IntActQ14573. 9 interactions.
MINTMINT-4991384.
STRING9606.ENSP00000363435.

Chemistry

BindingDBQ14573.
ChEMBLCHEMBL3904.
GuidetoPHARMACOLOGY745.

PTM databases

PhosphoSiteQ14573.

Polymorphism databases

DMDM209572633.

Proteomic databases

PaxDbQ14573.
PeptideAtlasQ14573.
PRIDEQ14573.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374316; ENSP00000363435; ENSG00000096433.
ENST00000605930; ENSP00000475177; ENSG00000096433.
GeneID3710.
KEGGhsa:3710.
UCSCuc021ywr.1. human.

Organism-specific databases

CTD3710.
GeneCardsGC06P033588.
H-InvDBHIX0005781.
HGNCHGNC:6182. ITPR3.
HPAHPA003915.
MIM147267. gene.
neXtProtNX_Q14573.
PharmGKBPA29980.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG280601.
HOGENOMHOG000007660.
HOVERGENHBG052158.
InParanoidQ14573.
KOK04960.
OMAKGDAKMM.
OrthoDBEOG76HQ0M.
PhylomeDBQ14573.
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

ArrayExpressQ14573.
BgeeQ14573.
CleanExHS_ITPR3.
GenevestigatorQ14573.

Family and domain databases

Gene3D1.25.10.30. 2 hits.
InterProIPR014821. 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.
SSF82109. SSF82109. 2 hits.
PROSITEPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITPR3. human.
GeneWikiITPR3.
GenomeRNAi3710.
NextBio14543.
PROQ14573.
SOURCESearch...

Entry information

Entry nameITPR3_HUMAN
AccessionPrimary (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: April 16, 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 6

Human chromosome 6: entries, gene names and cross-references to MIM