CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005819
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Inositol 1,4,5-trisphosphate receptor type 1 
Protein Synonyms/Alias
 IP3 receptor isoform 1; IP-3-R; IP3R 1; InsP3R1; Type 1 inositol 1,4,5-trisphosphate receptor; Type 1 InsP3 receptor 
Gene Name
 Itpr1 
Gene Synonyms/Alias
 Insp3r 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
91TDAVLLNKLHHAADLacetylation[1]
100HHAADLEKKQNETENacetylation[1]
424KIGTSPLKEDKEAFAubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional Description
 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). 
Sequence Annotation
 DOMAIN 112 166 MIR 1.
 DOMAIN 173 223 MIR 2.
 DOMAIN 231 287 MIR 3.
 DOMAIN 294 373 MIR 4.
 DOMAIN 379 435 MIR 5.
 REGION 265 269 Inositol 1,4,5-trisphosphate binding (By
 REGION 508 511 Inositol 1,4,5-trisphosphate binding (By
 REGION 567 569 Inositol 1,4,5-trisphosphate binding (By
 REGION 2464 2529 Interaction with ERP44.
 MOD_RES 482 482 Phosphotyrosine (Potential).
 MOD_RES 1589 1589 Phosphoserine (By similarity).
 MOD_RES 1756 1756 Phosphoserine; by PKA (Potential).
 MOD_RES 2656 2656 Phosphotyrosine (Potential).
 CROSSLNK 916 916 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 962 962 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1572 1572 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1772 1772 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1885 1885 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1886 1886 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1887 1887 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1902 1902 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1925 1925 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 2119 2119 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 2258 2258 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Apoptosis; Calcium; Calcium channel; Calcium transport; Complete proteome; Endoplasmic reticulum; Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2750 AA 
Protein Sequence
MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP KKFRDCLFKL 60
CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV 120
IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD 180
KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV 240
RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN 300
SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE 360
GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT 420
SPLKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL 480
VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE 540
LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH 600
NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT 660
NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW RDSNKEIRSK SVRELAQDAK 720
EGQKEDRDVL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS 780
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGASKDEIK ERFAQTMEFV 840
EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV 900
TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA PEGNVKQAEP 960
EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQSSE TSSGNSSQEG 1020
PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL 1080
QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD 1140
EPMDGASGEN EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ 1200
QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ NQALLHKHIN 1260
LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG 1320
KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LFMYHIHLVE 1380
LLAVCTEGKN VYTEIKCNSL LPLDDIVRVV THEDCIPEVK IAYINFLNHC YVDTEVEMKE 1440
IYTSNHMWKL FENFLVDICR ACNNTSDRKH ADSVLEKYVT EIVMSIVTTF FSSPFSDQST 1500
TLQTRQPVFV QLLQGVFRVY HCNWLMPSQK ASVESCIRVL SDVAKSRAIA IPVDLDSQVN 1560
NLFLKSHNIV QKTAMNWRLS ARNAARRDSV LAASRDYRNI IERLQDIVSA LEDRLRPLVQ 1620
AELSVLVDVL HRPELLFPEN TDARRKCESG GFICKLIKHT KQLLEENEEK LCIKVLQTLR 1680
EMMTKDRGYG EKQISIDELE NAELPQPPEA ENSTEQELEP SPPLRQLEDH KRGEALRQIL 1740
VNRYYGNIRP SGRRESLTSF GNGPLSPGGP SKPGGGGGGP GSGSTSRGEM SLAEVQCHLD 1800
KEGASNLVID LIMNASSDRV FHESILLAIA LLEGGNTTIQ HSFFCRLTED KKSEKFFKVF 1860
YDRMKVAQQE IKATVTVNTS DLGNKKKDDE VDRDAPSRKK AKEPTTQITE EVRDQLLEAS 1920
AATRKAFTTF RREADPDDHY QSGEGTQATT DKAKDDLEMS AVITIMQPIL RFLQLLCENH 1980
NRDLQNFLRC QNNKTNYNLV CETLQFLDCI CGSTTGGLGL LGLYINEKNV ALINQTLESL 2040
TEYCQGPCHE NQNCIATHES NGIDIITALI LNDINPLGKK RMDLVLELKN NASKLLLAIM 2100
ESRHDSENAE RILYNMRPKE LVEVIKKAYM QGEVEFEDGE NGEDGAASPR NVGHNIYILA 2160
HQLARHNKEL QTMLKPGGQV DGDEALEFYA KHTAQIEIVR LDRTMEQIVF PVPSICEFLT 2220
KESKLRIYYT TERDEQGSKI NDFFLRSEDL FNEMNWQKKL RAQPVLYWCA RNMSFWSSIS 2280
FNLAVLMNLL VAFFYPFKGV RGGTLEPHWS GLLWTAMLIS LAIVIALPKP HGIRALIAST 2340
ILRLIFSVGL QPTLFLLGAF NVCNKIIFLM SFVGNCGTFT RGYRAMVLDV EFLYHLLYLL 2400
ICAMGLFVHE FFYSLLLFDL VYREETLLNV IKSVTRNGRP IILTAALALI LVYLFSIVGY 2460
LFFKDDFILE VDRLPNETAG PETGESLAND FLYSDVCRVE TGENCTSPAP KEELLPVEET 2520
EQDKEHTCET LLMCIVTVLS HGLRSGGGVG DVLRKPSKEE PLFAARVIYD LLFFFMVIII 2580
VLNLIFGVII DTFADLRSEK QKKEEILKTT CFICGLERDK FDNKTVTFEE HIKEEHNMWH 2640
YLCFIVLVKV KDSTEYTGPE SYVAEMIRER NLDWFPRMRA MSLVSSDSEG EQNELRNLQE 2700
KLESTMKLVT NLSGQLSELK DQMTEQRKQK QRIGLLGHPP HMNVNPQQPA 2750 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0045121; C:membrane raft; IDA:RGD.
 GO:0043025; C:neuronal cell body; IDA:RGD.
 GO:0005635; C:nuclear envelope; IDA:RGD.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
 GO:0005886; C:plasma membrane; IDA:RGD.
 GO:0014069; C:postsynaptic density; IDA:RGD.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0016529; C:sarcoplasmic reticulum; IDA:RGD.
 GO:0030667; C:secretory granule membrane; IDA:RGD.
 GO:0097060; C:synaptic membrane; IDA:RGD.
 GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; ISS:UniProtKB.
 GO:0005218; F:intracellular ligand-gated calcium channel activity; ISS:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
 GO:0032403; F:protein complex binding; IDA:RGD.
 GO:0019903; F:protein phosphatase binding; IDA:RGD.
 GO:0071320; P:cellular response to cAMP; IDA:RGD.
 GO:0071456; P:cellular response to hypoxia; IEP:RGD.
 GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
 GO:1901215; P:negative regulation of neuron death; IMP:RGD.
 GO:0051928; P:positive regulation of calcium ion transport; IDA:RGD.
 GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:BHF-UCL. 
Interpro
 IPR000699; Ca-rel_channel.
 IPR014821; Ins145_P3_rcpt.
 IPR000493; InsP3_rcpt-bd.
 IPR005821; Ion_trans_dom.
 IPR016093; MIR_motif.
 IPR013662; RIH_assoc-dom.
 IPR015925; Ryanodine_recept-rel. 
Pfam
 PF08709; Ins145_P3_rec
 PF00520; Ion_trans
 PF02815; MIR
 PF08454; RIH_assoc
 PF01365; RYDR_ITPR 
SMART
 SM00472; MIR 
PROSITE
 PS50919; MIR 
PRINTS
 PR00779; INSP3RECEPTR.