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P29994 (ITPR1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol 1,4,5-trisphosphate receptor type 1
Alternative name(s):
IP3 receptor isoform 1
Short name=IP-3-R
Short name=IP3R 1
Short name=InsP3R1
Type 1 inositol 1,4,5-trisphosphate receptor
Short name=Type 1 InsP3 receptor
Gene names
Name:Itpr1
Synonyms:Insp3r
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length2750 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Plays a role in ER stress-induced apoptosis. Cytoplasmic calcium released from the ER triggers apoptosis by the activation of CaM kinase II, eventually leading to the activation of downstream apoptosis pathways By similarity.

Subunit structure

Homotetramer. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1. Interacts with TRPC4. The PPXXF motif binds HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3. Interacts with ERP44 in a pH-, redox state- and calcium-dependent manner which results in the inhibition the calcium channel activity. The strength of this interaction inversely correlates with calcium concentration. Interacts with CABP1. Interacts with AHCYL1 and MRVI1 By similarity. Interacts with TESPA1 By similarity. Ref.5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Tissue specificity

Isoform 3 is found in the brain while isoform 7 is found in the fetal brain and peripheral tissues.

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 by cAMP kinase. Phosphorylation prevents the ligand-induced opening of the calcium channels.

Phosphorylated on tyrosine residues By similarity.

Ubiquitination at multiple lysines targets ITPR1 for proteasomal degradation. Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked.

Miscellaneous

Calcium appears to inhibit ligand binding to the receptor, most probably by interacting with a distinct calcium-binding protein which then inhibits the receptor.

Sequence similarities

Belongs to the InsP3 receptor family.

Contains 5 MIR domains.

Ontologies

Keywords
   Biological processApoptosis
Calcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
Ligand-gated ion channel
Receptor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to cAMP

Inferred from direct assay PubMed 20189985. Source: RGD

cellular response to hypoxia

Inferred from expression pattern PubMed 17285299. Source: RGD

inositol phosphate-mediated signaling

Inferred from direct assay PubMed 15533917PubMed 19036964. Source: GOC

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron death

Inferred from mutant phenotype PubMed 20434434. Source: RGD

positive regulation of calcium ion transport

Inferred from direct assay PubMed 19036964. Source: RGD

positive regulation of cytosolic calcium ion concentration

Inferred from mutant phenotype PubMed 15911880. Source: RGD

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype PubMed 16223735. Source: BHF-UCL

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12615969. Source: RGD

dendrite

Inferred from direct assay PubMed 17471556. Source: RGD

endoplasmic reticulum membrane

Inferred from direct assay PubMed 15533917PubMed 15911880. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 21859719. Source: RGD

membrane raft

Inferred from direct assay PubMed 15911880. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 17471556. Source: RGD

nuclear envelope

Inferred from direct assay PubMed 16014380. Source: RGD

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12615969. Source: RGD

plasma membrane

Inferred from direct assay PubMed 15911880. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 1338970. Source: RGD

protein complex

Inferred from direct assay PubMed 12676536. Source: RGD

sarcoplasmic reticulum

Inferred from direct assay PubMed 16014380. Source: RGD

secretory granule membrane

Inferred from direct assay PubMed 15911880. Source: RGD

synaptic membrane

Inferred from direct assay PubMed 12676536. Source: RGD

   Molecular_functioninositol 1,4,5-trisphosphate-sensitive calcium-release channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular ligand-gated calcium channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction PubMed 12676536. Source: RGD

protein binding

Inferred from physical interaction PubMed 12873381PubMed 15911880PubMed 16103111PubMed 19036964. Source: RGD

protein complex binding

Inferred from direct assay PubMed 15212990. Source: RGD

protein phosphatase binding

Inferred from direct assay PubMed 15212990. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: There is a combination of two alternatively spliced domains at site SI and site SII (A, B and C). Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: P29994-1)

Also known as: SISIIABC;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P29994-2)

Also known as: SI-SIIABC;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
Isoform 3 (identifier: P29994-3)

Also known as: SISIIAC;

The sequence of this isoform differs from the canonical sequence as follows:
     1716-1716: Missing.
Isoform 4 (identifier: P29994-4)

Also known as: SI-SIIAC;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     1716-1716: Missing.
Isoform 5 (identifier: P29994-5)

Also known as: SISIIA;

The sequence of this isoform differs from the canonical sequence as follows:
     1716-1716: Missing.
     1717-1732: Missing.
Isoform 6 (identifier: P29994-6)

Also known as: SI-SIIA;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     1716-1716: Missing.
     1717-1732: Missing.
Isoform 7 (identifier: P29994-7)

Also known as: SISII;

The sequence of this isoform differs from the canonical sequence as follows:
     1693-1715: Missing.
     1716-1716: Missing.
     1717-1732: Missing.
Isoform 8 (identifier: P29994-8)

Also known as: SI-SII;

The sequence of this isoform differs from the canonical sequence as follows:
     322-336: Missing.
     1693-1715: Missing.
     1716-1716: Missing.
     1717-1732: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 27502750Inositol 1,4,5-trisphosphate receptor type 1
PRO_0000153922

Regions

Topological domain1 – 22742274Cytoplasmic Potential
Transmembrane2275 – 229521Helical; Potential
Topological domain2296 – 230611Lumenal Potential
Transmembrane2307 – 232721Helical; Potential
Topological domain2328 – 235326Cytoplasmic Potential
Transmembrane2354 – 237421Helical; Potential
Topological domain2375 – 239723Lumenal Potential
Transmembrane2398 – 241821Helical; Potential
Topological domain2419 – 244022Cytoplasmic Potential
Transmembrane2441 – 246121Helical; Potential
Topological domain2462 – 2569108Lumenal Potential
Transmembrane2570 – 259021Helical; Potential
Topological domain2591 – 2750160Cytoplasmic Potential
Domain112 – 16655MIR 1
Domain173 – 22351MIR 2
Domain231 – 28757MIR 3
Domain294 – 37380MIR 4
Domain379 – 43557MIR 5
Region265 – 2695Inositol 1,4,5-trisphosphate binding By similarity
Region508 – 5114Inositol 1,4,5-trisphosphate binding By similarity
Region567 – 5693Inositol 1,4,5-trisphosphate binding By similarity
Region2464 – 252966Interaction with ERP44

Amino acid modifications

Modified residue4821Phosphotyrosine Potential
Modified residue15891Phosphoserine By similarity
Modified residue17561Phosphoserine; by PKA Potential
Modified residue26561Phosphotyrosine Potential
Cross-link916Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link962Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link1572Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link1772Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link1885Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link1886Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link1887Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link1902Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link1925Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link2119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6
Cross-link2258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6

Natural variations

Alternative sequence322 – 33615Missing in isoform 2, isoform 4, isoform 6 and isoform 8.
VSP_002695
Alternative sequence1693 – 171523Missing in isoform 7 and isoform 8.
VSP_002696
Alternative sequence17161Missing in isoform 3, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_002697
Alternative sequence1717 – 173216Missing in isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_002698
Natural variant13721Missing in all but PI17 clones. Ref.1

Experimental info

Sequence conflict17641P → R in AAA41447. Ref.2
Sequence conflict17641P → R in AAA41448. Ref.2

Secondary structure

..................................................................................... 2750
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SISIIABC) [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: 174BB77CBF6F21AC

FASTA2,750313,264
        10         20         30         40         50         60 
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP KKFRDCLFKL 

        70         80         90        100        110        120 
CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV 

       130        140        150        160        170        180 
IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD 

       190        200        210        220        230        240 
KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV 

       250        260        270        280        290        300 
RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN 

       310        320        330        340        350        360 
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE 

       370        380        390        400        410        420 
GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT 

       430        440        450        460        470        480 
SPLKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL 

       490        500        510        520        530        540 
VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE 

       550        560        570        580        590        600 
LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH 

       610        620        630        640        650        660 
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT 

       670        680        690        700        710        720 
NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW RDSNKEIRSK SVRELAQDAK 

       730        740        750        760        770        780 
EGQKEDRDVL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS 

       790        800        810        820        830        840 
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGASKDEIK ERFAQTMEFV 

       850        860        870        880        890        900 
EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV 

       910        920        930        940        950        960 
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA PEGNVKQAEP 

       970        980        990       1000       1010       1020 
EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQSSE TSSGNSSQEG 

      1030       1040       1050       1060       1070       1080 
PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL 

      1090       1100       1110       1120       1130       1140 
QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD 

      1150       1160       1170       1180       1190       1200 
EPMDGASGEN EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ 

      1210       1220       1230       1240       1250       1260 
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ NQALLHKHIN 

      1270       1280       1290       1300       1310       1320 
LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG 

      1330       1340       1350       1360       1370       1380 
KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LFMYHIHLVE 

      1390       1400       1410       1420       1430       1440 
LLAVCTEGKN VYTEIKCNSL LPLDDIVRVV THEDCIPEVK IAYINFLNHC YVDTEVEMKE 

      1450       1460       1470       1480       1490       1500 
IYTSNHMWKL FENFLVDICR ACNNTSDRKH ADSVLEKYVT EIVMSIVTTF FSSPFSDQST 

      1510       1520       1530       1540       1550       1560 
TLQTRQPVFV QLLQGVFRVY HCNWLMPSQK ASVESCIRVL SDVAKSRAIA IPVDLDSQVN 

      1570       1580       1590       1600       1610       1620 
NLFLKSHNIV QKTAMNWRLS ARNAARRDSV LAASRDYRNI IERLQDIVSA LEDRLRPLVQ 

      1630       1640       1650       1660       1670       1680 
AELSVLVDVL HRPELLFPEN TDARRKCESG GFICKLIKHT KQLLEENEEK LCIKVLQTLR 

      1690       1700       1710       1720       1730       1740 
EMMTKDRGYG EKQISIDELE NAELPQPPEA ENSTEQELEP SPPLRQLEDH KRGEALRQIL 

      1750       1760       1770       1780       1790       1800 
VNRYYGNIRP SGRRESLTSF GNGPLSPGGP SKPGGGGGGP GSGSTSRGEM SLAEVQCHLD 

      1810       1820       1830       1840       1850       1860 
KEGASNLVID LIMNASSDRV FHESILLAIA LLEGGNTTIQ HSFFCRLTED KKSEKFFKVF 

      1870       1880       1890       1900       1910       1920 
YDRMKVAQQE IKATVTVNTS DLGNKKKDDE VDRDAPSRKK AKEPTTQITE EVRDQLLEAS 

      1930       1940       1950       1960       1970       1980 
AATRKAFTTF RREADPDDHY QSGEGTQATT DKAKDDLEMS AVITIMQPIL RFLQLLCENH 

      1990       2000       2010       2020       2030       2040 
NRDLQNFLRC QNNKTNYNLV CETLQFLDCI CGSTTGGLGL LGLYINEKNV ALINQTLESL 

      2050       2060       2070       2080       2090       2100 
TEYCQGPCHE NQNCIATHES NGIDIITALI LNDINPLGKK RMDLVLELKN NASKLLLAIM 

      2110       2120       2130       2140       2150       2160 
ESRHDSENAE RILYNMRPKE LVEVIKKAYM QGEVEFEDGE NGEDGAASPR NVGHNIYILA 

      2170       2180       2190       2200       2210       2220 
HQLARHNKEL QTMLKPGGQV DGDEALEFYA KHTAQIEIVR LDRTMEQIVF PVPSICEFLT 

      2230       2240       2250       2260       2270       2280 
KESKLRIYYT TERDEQGSKI NDFFLRSEDL FNEMNWQKKL RAQPVLYWCA RNMSFWSSIS 

      2290       2300       2310       2320       2330       2340 
FNLAVLMNLL VAFFYPFKGV RGGTLEPHWS GLLWTAMLIS LAIVIALPKP HGIRALIAST 

      2350       2360       2370       2380       2390       2400 
ILRLIFSVGL QPTLFLLGAF NVCNKIIFLM SFVGNCGTFT RGYRAMVLDV EFLYHLLYLL 

      2410       2420       2430       2440       2450       2460 
ICAMGLFVHE FFYSLLLFDL VYREETLLNV IKSVTRNGRP IILTAALALI LVYLFSIVGY 

      2470       2480       2490       2500       2510       2520 
LFFKDDFILE VDRLPNETAG PETGESLAND FLYSDVCRVE TGENCTSPAP KEELLPVEET 

      2530       2540       2550       2560       2570       2580 
EQDKEHTCET LLMCIVTVLS HGLRSGGGVG DVLRKPSKEE PLFAARVIYD LLFFFMVIII 

      2590       2600       2610       2620       2630       2640 
VLNLIFGVII DTFADLRSEK QKKEEILKTT CFICGLERDK FDNKTVTFEE HIKEEHNMWH 

      2650       2660       2670       2680       2690       2700 
YLCFIVLVKV KDSTEYTGPE SYVAEMIRER NLDWFPRMRA MSLVSSDSEG EQNELRNLQE 

      2710       2720       2730       2740       2750 
KLESTMKLVT NLSGQLSELK DQMTEQRKQK QRIGLLGHPP HMNVNPQQPA 

« Hide

Isoform 2 (SI-SIIABC) [UniParc].

Checksum: A80CC16884635058
Show »

FASTA2,735311,498
Isoform 3 (SISIIAC) [UniParc].

Checksum: E80D784F7201E2C9
Show »

FASTA2,749313,136
Isoform 4 (SI-SIIAC) [UniParc].

Checksum: EF7B6C747E701605
Show »

FASTA2,734311,370
Isoform 5 (SISIIA) [UniParc].

Checksum: 3BE4A15DD99264F5
Show »

FASTA2,733311,210
Isoform 6 (SI-SIIA) [UniParc].

Checksum: FBE35154A6AF0190
Show »

FASTA2,718309,444
Isoform 7 (SISII) [UniParc].

Checksum: 6A7FF31BC8448BFD
Show »

FASTA2,710308,674
Isoform 8 (SI-SII) [UniParc].

Checksum: 81B8B4551AB0814F
Show »

FASTA2,695306,909

References

[1]"Structure and expression of the rat inositol 1,4,5-trisphosphate receptor."
Mignery G.A., Newton C.L., Archer B.T. III, Suedhof T.C.
J. Biol. Chem. 265:12679-12685(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), VARIANT PHE-1372 DEL.
[2]"Inositol 1,4,5-trisphosphate receptors: distinct neuronal and nonneuronal forms derived by alternative splicing differ in phosphorylation."
Danoff S.K., Ferris C.D., Donath C., Fischer G.A., Munemitsu S., Ullrich A., Snyder S.H., Ross C.A.
Proc. Natl. Acad. Sci. U.S.A. 88:2951-2955(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 7).
Tissue: Brain.
[3]"Inositol 1,4,5-trisphosphate receptor expression in mammalian olfactory tissue."
Smutzer G., Zimmerman J.E., Hahn C.-G., Ruscheinsky D.D., Rodriguez A., Han L.-Y., Arnold S.E.
Brain Res. Mol. Brain Res. 44:347-354(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 7 AND 8).
Strain: Sprague-Dawley.
[4]"Subunit oligomerization, and topology of the inositol 1,4, 5-trisphosphate receptor."
Galvan D.L., Borrego-Diaz E., Perez P.J., Mignery G.A.
J. Biol. Chem. 274:29483-29492(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[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]"Mass spectrometric analysis of type 1 inositol 1,4,5-trisphosphate receptor ubiquitination."
Sliter D.A., Kubota K., Kirkpatrick D.S., Alzayady K.J., Gygi S.P., Wojcikiewicz R.J.
J. Biol. Chem. 283:35319-35328(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-916; LYS-962; LYS-1572; LYS-1772; LYS-1885; LYS-1886; LYS-1887; LYS-1902; LYS-1925; LYS-2119 AND LYS-2258.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05510 mRNA. Translation: AAA41358.1.
J05510 mRNA. Translation: AAA41357.1.
M64699 mRNA. Translation: AAA41447.1.
M64698 mRNA. Translation: AAA41448.1.
U38653 mRNA. Translation: AAC53099.1.
U38812 mRNA. Translation: AAC53100.1.
U38665 mRNA. Translation: AAB51330.1.
PIRA36579.
B36579.
RefSeqNP_001257526.1. NM_001270597.1.
UniGeneRn.2135.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3T8SX-ray3.77A/B7-602[»]
3UJ0X-ray3.60A/B1-604[»]
3UJ4X-ray3.00A/B1-604[»]
ProteinModelPortalP29994.
SMRP29994. Positions 7-225, 236-602.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247302. 11 interactions.
DIPDIP-29715N.
IntActP29994. 1 interaction.
MINTMINT-5026585.

Chemistry

BindingDBP29994.
ChEMBLCHEMBL2804.

PTM databases

PhosphoSiteP29994.

Proteomic databases

PaxDbP29994.
PRIDEP29994.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25262.
KEGGrno:25262.

Organism-specific databases

CTD3708.
RGD2933. Itpr1.

Phylogenomic databases

eggNOGNOG280601.
HOGENOMHOG000007660.
HOVERGENHBG052158.
InParanoidP29994.
KOK04958.
PhylomeDBP29994.

Enzyme and pathway databases

ReactomeREACT_205051. Metabolism.
REACT_206767. Disease.
REACT_212996. Signal Transduction.
REACT_227097. Immune System.

Gene expression databases

GenevestigatorP29994.

Family and domain databases

Gene3D1.25.10.30. 2 hits.
InterProIPR016024. ARM-type_fold.
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]
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.
SSF48371. SSF48371. 4 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio605915.
PROP29994.

Entry information

Entry nameITPR1_RAT
AccessionPrimary (citable) accession number: P29994
Secondary accession number(s): Q62869
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 2, 2001
Last modified: June 11, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references