CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003977
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]
427TSPLKEDKEAFAIVPubiquitination[1]
451DFANDASKVLGSIAGubiquitination[1]
462SIAGKLEKGTITQNEubiquitination[1]
517MREQNILKQIFKLLQubiquitination[1]
569HSQQDYRKNQEYIAKphosphoglycerylation[2]
861FSDKEKNKLTFEVVNubiquitination[1]
971DIMVMDTKLKIIEILubiquitination[1]
1128QLRSIVEKSELWVYKubiquitination[1]
1310GRNVQYIKFLQTIVKubiquitination[1]
1317KFLQTIVKAEGKFIKubiquitination[1]
1654ESGGFICKLIKHTKQubiquitination[1]
1660CKLIKHTKQLLEENEubiquitination[1]
1673NEEKLCIKVLQTLREubiquitination[1]
1857KKSEKFFKVFYDRMKubiquitination[1]
2118ILYNMRPKELVEVIKubiquitination[1]
2167HQLARHNKELQTMLKubiquitination[1]
2238ERDEQGSKINDFFLRubiquitination[1]
2257FNEMNWQKKLRAQPVubiquitination[1]
2700ELRNLQEKLESTMKLubiquitination[1]
2706EKLESTMKLVTNLSGubiquitination[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]
 [2] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237] 
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 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
EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS 780
FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGTSKDEIK 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 LMYHIHLVEL 1380
LAVCTEGKNV YTEIKCNSLL PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI 1440
YTSNHMWKLF ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT 1500
LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI PVDLDSQVNN 1560
LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII ERLQDIVSAL EDRLRPLVQA 1620
ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL CIKVLQTLRE 1680
MMTKDRGYGE KQISIDESEN AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV 1740
NRYYGNIRPS GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK 1800
EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK KSEKFFKVFY 1860
DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA KEPTTQITEE VRDQLLEASA 1920
ATRKAFTTFR READPDDHYQ SGEGTQATTD KAKDDLEMSA VITIMQPILR FLQLLCENHN 1980
RDLQNFLRCQ NNKTNYNLVC ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT 2040
EYCQGPCHEN QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME 2100
SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN VGHNIYILAH 2160
QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL DRTMEQIVFP VPSICEFLTK 2220
ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF NEMNWQKKLR AQPVLYWCAR NMSFWSSISF 2280
NLAVLMNLLV AFFYPFKGVR GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI 2340
LRLIFSVGLQ PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI 2400
CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL VYLFSIVGYL 2460
FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET GENCTSPAPK EELLPAEETE 2520
QDKEHTCETL LMCIVTVLSH GLRSGGGVGD VLRKPSKEEP LFAARVIYDL LFFFMVIIIV 2580
LNLIFGVIID TFADLRSEKQ KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY 2640
LCFIVLVKVK DSTEYTGPES YVAEMIRERN LDWFPRMRAM SLVSSDSEGE QNELRNLQEK 2700
LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA 2749 
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.