CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003978
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; IP3R 1; InsP3R1; Inositol 1,4,5-trisphosphate-binding protein P400; Protein PCD-6; Purkinje cell protein 1; Type 1 inositol 1,4,5-trisphosphate receptor; Type 1 InsP3 receptor 
Gene Name
 Itpr1 
Gene Synonyms/Alias
 Insp3r; Pcd6; Pcp1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
77KQFWKAAKPGANSTTubiquitination[1]
279ATSATSSKALWEVEVubiquitination[1]
306WNSLFRFKHLATGHYubiquitination[1]
412TSPLKEDKEAFAIVPubiquitination[1]
436DFANDASKVLGSIAGubiquitination[1]
447SIAGKLEKGTITQNEubiquitination[1]
502MREQNILKQIFKLLQubiquitination[1]
846FSDKEKNKLTFEVVNubiquitination[1]
956DIMVMDTKLKIIEILubiquitination[1]
1113QLRSIVEKSELWVYKubiquitination[1]
1295GRNVQYIKFLQTIVKubiquitination[1]
1302KFLQTIVKAEGKFIKubiquitination[1]
1639ESGGFICKLIKHTKQubiquitination[1]
1645CKLIKHTKQLLEENEubiquitination[1]
1658NEEKLCIKVLQTLREubiquitination[1]
1842KKSEKFFKVFYDRMKubiquitination[1]
2103ILYNMRPKELVEVIKubiquitination[1]
2152HQLARHNKELQTMLKubiquitination[1]
2223ERDEQGSKINDFFLRubiquitination[1]
2242FNEMNWQKKLRAQPVubiquitination[1]
2685ELRNLQEKLESTMKLubiquitination[1]
2691EKLESTMKLVTNLSGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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. 
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.
 REGION 508 511 Inositol 1,4,5-trisphosphate binding.
 REGION 567 569 Inositol 1,4,5-trisphosphate binding.
 REGION 2463 2528 Interaction with ERP44.
 MOD_RES 482 482 Phosphotyrosine (Potential).
 MOD_RES 1588 1588 Phosphoserine.
 MOD_RES 1755 1755 Phosphoserine; by PKA (Potential).
 MOD_RES 2655 2655 Phosphotyrosine (Potential).
 CROSSLNK 916 916 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 962 962 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1571 1571 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1771 1771 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1884 1884 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1885 1885 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1886 1886 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1901 1901 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 1924 1924 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 2118 2118 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 2257 2257 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Alternative splicing; Apoptosis; Calcium; Calcium channel; Calcium transport; Complete proteome; Direct protein sequencing; 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
 2749 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 DQDASRSRLR NAQEKMVYSL VSVPEGNDIS SIFELDPTTL 360
RGGDSLVPRN SYVRLRHLCT NTWVHSTNIP IDKEEEKPVM LKIGTSPLKE DKEAFAIVPV 420
SPAEVRDLDF ANDASKVLGS IAGKLEKGTI TQNERRSVTK LLEDLVYFVT GGTNSGQDVL 480
EVVFSKPNRE RQKLMREQNI LKQIFKLLQA PFTDCGDGPM LRLEELGDQR HAPFRHICRL 540
CYRVLRHSQQ DYRKNQEYIA KQFGFMQKQI GYDVLAEDTI TALLHNNRKL LEKHITAAEI 600
DTFVSLVRKN REPRFLDYLS DLCVSMNKSI PVTQELICKA VLNPTNADIL IETKLVLSRF 660
EFEGVSTGEN ALEAGEDEEE VWLFWRDSNK EIRSKSVREL AQDAKEGQKE DRDILSYYRY 720
QLNLFARMCL DRQYLAINEI SGQLDVDLIL RCMSDENLPY DLRASFCRLM LHMHVDRDPQ 780
EQVTPVKYAR LWSEIPSEIA IDDYDSSGTS KDEIKERFAQ TMEFVEEYLR DVVCQRFPFS 840
DKEKNKLTFE VVNLARNLIY FGFYNFSDLL RLTKILLAIL DCVHVTTIFP ISKMTKGEEN 900
KGSNVMRSIH GVGELMTQVV LRGGGFLPMT PMAAAPEGNV KQAEPEKEDI MVMDTKLKII 960
EILQFILNVR LDYRISCLLC IFKREFDESN SQSSETSSGN SSQEGPSNVP GALDFEHIEE 1020
QAEGIFGGSE ENTPLDLDDH GGRTFLRVLL HLTMHDYPPL VSGALQLLFR HFSQRQEVLQ 1080
AFKQVQLLVT SQDVDNYKQI KQDLDQLRSI VEKSELWVYK GQGPDEPMDG ASGENEHKKT 1140
EEGTSKPLKH ESTSSYNYRV VKEILIRLSK LCVQESASVR KSRKQQQRLL RNMGAHAVVL 1200
ELLQIPYEKA EDTKMQEIMR LAHEFLQNFC AGNQQNQALL HKHINLFLNP GILEAVTMQH 1260
IFMNNFQLCS EINERVVQHF VHCIETHGRN VQYIKFLQTI VKAEGKFIKK CQDMVMAELV 1320
NSGEDVLVFY NDRASFQTLI QMMRSERDRM DENSPLMYHI HLVELLAVCT EGKNVYTEIK 1380
CNSLLPLDDI VRVVTHEDCI PEVKIAYINF LNHCYVDTEV EMKEIYTSNH MWKLFENFLV 1440
DICRACNNTS DRKHADSILE KYVTEIVMSI VTTFFSSPFS DQSTTLQTRQ PVFVQLLQGV 1500
FRVYHCNWLM PSQKASVESC IRVLSDVAKS RAIAIPVDLD SQVNNLFLKS HNIVQKTALN 1560
WRLSARNAAR RDSVLAASRD YRNIIERLQD IVSALEDRLR PLVQAELSVL VDVLHRPELL 1620
FPENTDARRK CESGGFICKL IKHTKQLLEE NEEKLCIKVL QTLREMMTKD RGYGEKQISI 1680
DESENAELPQ APEAENSTEQ ELEPSPPLRQ LEDHKRGEAL RQILVNRYYG NIRPSGRRES 1740
LTSFGNGPLS PGGPSKPGGG GGGPGSSSTS RGEMSLAEVQ CHLDKEGASN LVIDLIMNAS 1800
SDRVFHESIL LAIALLEGGN TTIQHSFFCR LTEDKKSEKF FKVFYDRMKV AQQEIKATVT 1860
VNTSDLGNKK KDDEVDRDAP SRKKAKEPTT QITEEVRDQL LEASAATRKA FTTFRREADP 1920
DDHYQSGEGT QATTDKAKDD LEMSAVITIM QPILRFLQLL CENHNRDLQN FLRCQNNKTN 1980
YNLVCETLQF LDCICGSTTG GLGLLGLYIN EKNVALINQT LESLTEYCQG PCHENQNCIA 2040
THESNGIDII TALILNDINP LGKKRMDLVL ELKNNASKLL LAIMESRHDS ENAERILYNM 2100
RPKELVEVIK KAYMQGEVEF EDGENGEDGA ASPRNVGHNI YILAHQLARH NKELQTMLKP 2160
GGQVDGDEAL EFYAKHTAQI EIVRLDRTME QIVFPVPSIC EFLTKESKLR IYYTTERDEQ 2220
GSKINDFFLR SEDLFNEMNW QKKLRAQPVL YWCARNMSFW SSISFNLAVL MNLLVAFFYP 2280
FKGVRGGTLE PHWSGLLWTA MLISLAIVIA LPKPHGIRAL IASTILRLIF SVGLQPTLFL 2340
LGAFNVCNKI IFLMSFVGNC GTFTRGYRAM VLDVEFLYHL LYLLICAMGL FVHEFFYSLL 2400
LFDLVYREET LLNVIKSVTR NGRSIILTAV LALILVYLFS IVGYLFFKDD FILEVDRLPN 2460
ETAVPETGES LANDFLYSDV CRVETGENCT SPAPKEELLP AEETEQDKEH TCETLLMCIV 2520
TVLSHGLRSG GGVGDVLRKP SKEEPLFAAR VIYDLLFFFM VIIIVLNLIF GVIIDTFADL 2580
RSEKQKKEEI LKTTCFICGL ERDKFDNKTV TFEEHIKEEH NMWHYLCFIV LVKVKDSTEY 2640
TGPESYVAEM IRERNLDWFP RMRAMSLVSS DSEGEQNELR NLQEKLESTM KLVTNLSGQL 2700
SELKDQMTEQ RKQKQRIGLL GHPPHMNVNP QQPA 2734 
Gene Ontology
 GO:0005955; C:calcineurin complex; IDA:MGI.
 GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005637; C:nuclear inner membrane; IDA:MGI.
 GO:0005730; C:nucleolus; IDA:MGI.
 GO:0014069; C:postsynaptic density; IDA:MGI.
 GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
 GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB.
 GO:0005218; F:intracellular ligand-gated calcium channel activity; IDA:UniProtKB.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
 GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
 GO:0009791; P:post-embryonic development; IMP:MGI.
 GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:UniProtKB.
 GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
 GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI. 
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.