ITPR1_MOUSE - dbPTM
ITPR1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITPR1_MOUSE
UniProt AC P11881
Protein Name Inositol 1,4,5-trisphosphate receptor type 1
Gene Name Itpr1
Organism Mus musculus (Mouse).
Sequence Length 2749
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Cytoplasmic vesicle, secretory vesicle membrane
Multi-pass membrane protein . Cytoplasm, perinuclear region . Endoplasmic reticulum and secretory granules (By similarity).
Protein Description Intracellular channel that mediates calcium release from the endoplasmic reticulum following stimulation by inositol 1,4,5-trisphosphate. Involved in the regulation of epithelial secretion of electrolytes and fluid through the interaction with AHCYL1. [PubMed: 23542070 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.]
Protein Sequence MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDILSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGTSKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSILEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTALNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDESENAELPQAPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSSSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLPNETAVPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPAEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
56S-palmitoylationPPKKFRDCLFKLCPM
CCHHHHHHHHHHCCC		4.1325368151
77UbiquitinationKQFWKAAKPGANSTT
HHHHHHCCCCCCCCH		49.1722790023
77 (in isoform 2)Ubiquitination-49.1722790023
131PhosphorylationLHLKSNKYLTVNKRL
EECCCCCCCEECCCH		16.32-
133PhosphorylationLKSNKYLTVNKRLPA
CCCCCCCEECCCHHH		20.95-
225AcetylationWKIVLFMKWSDNKDD
EEEEEEEEECCCHHH		35.8919856637
279UbiquitinationATSATSSKALWEVEV
CCCCCCCCCEEEEEE		47.4622790023
279 (in isoform 2)Ubiquitination-47.4622790023
306UbiquitinationWNSLFRFKHLATGHY
HHHHHHHHHHHCCCE		33.1922790023
306 (in isoform 2)Ubiquitination-33.1922790023
353PhosphorylationNAQEKMVYSLVSVPE
HHHHHHHEEEEECCC		7.8720814235
412 (in isoform 2)Ubiquitination-46.31-
421PhosphorylationVMLKIGTSPLKEDKE
CEEEEECCCCCCCCC		24.0322817900
427UbiquitinationTSPLKEDKEAFAIVP
CCCCCCCCCEEEEEE		52.6222790023
427 (in isoform 2)Ubiquitination-52.6222790023
436PhosphorylationAFAIVPVSPAEVRDL
EEEEEECCHHHHCCC		16.6022817900
436 (in isoform 2)Ubiquitination-16.60-
447 (in isoform 2)Ubiquitination-45.43-
451UbiquitinationDFANDASKVLGSIAG
CCCCCHHHHHHHHHH		43.1022790023
451 (in isoform 2)Ubiquitination-43.1022790023
462UbiquitinationSIAGKLEKGTITQNE
HHHHHCCCCCCCHHH		72.3222790023
462 (in isoform 2)Ubiquitination-72.3222790023
482PhosphorylationKLLEDLVYFVTGGTN
HHHHHHCHHHHCCCC		10.30-
502 (in isoform 2)Ubiquitination-43.86-
517UbiquitinationMREQNILKQIFKLLQ
HHHHHHHHHHHHHHH		37.2322790023
517 (in isoform 2)Ubiquitination-37.2322790023
569MalonylationHSQQDYRKNQEYIAK
HHHHHHHHCHHHHHH		57.6726320211
569PhosphoglycerylationHSQQDYRKNQEYIAK
HHHHHHHHCHHHHHH		57.67-
799PhosphorylationRDPQEQVTPVKYARL
CCHHHCCCCCHHHHH		23.2722817900
846 (in isoform 2)Ubiquitination-34.31-
849S-palmitoylationEYLRDVVCQRFPFSD
HHHHHHHHHHCCCCH		2.1125368151
861UbiquitinationFSDKEKNKLTFEVVN
CCHHHCCCCCHHHHH		61.0322790023
861 (in isoform 2)Ubiquitination-61.0322790023
916UbiquitinationMTKGEENKGSNVMRS
CCCCCCCCCCCHHHH		67.98-
945PhosphorylationGGGFLPMTPMAAAPE
CCCCCCCCCCCCCCC		14.15-
956 (in isoform 2)Ubiquitination-48.03-
962UbiquitinationVKQAEPEKEDIMVMD
CCCCCCCHHCCEEEC		71.98-
971UbiquitinationDIMVMDTKLKIIEIL
CCEEECCHHHHHHHH		43.4422790023
971 (in isoform 2)Ubiquitination-43.4422790023
1113 (in isoform 2)Ubiquitination-52.37-
1128UbiquitinationQLRSIVEKSELWVYK
HHHHHHHHHHEEEEE		38.0322790023
1128 (in isoform 2)Ubiquitination-38.0322790023
1147PhosphorylationDEPMDGASGENEHKK
CCCCCCCCCCCCCCC		52.7723684622
1167PhosphorylationSKPLKHESTSSYNYR
CCCCCCCCCCCCCHH		33.0523684622
1191PhosphorylationSKLCVQESASVRKSR
HHHHHHHCHHHHHHH		14.5730635358
1193PhosphorylationLCVQESASVRKSRKQ
HHHHHCHHHHHHHHH		31.5630635358
1295 (in isoform 2)Ubiquitination-1.93-
1302 (in isoform 2)Ubiquitination-22.04-
1310UbiquitinationGRNVQYIKFLQTIVK
CCCHHHHHHHHHHHH		34.7822790023
1310 (in isoform 2)Ubiquitination-34.7822790023
1317UbiquitinationKFLQTIVKAEGKFIK
HHHHHHHHHCCHHHH		36.5522790023
1317 (in isoform 2)Ubiquitination-36.5522790023
1443PhosphorylationEMKEIYTSNHMWKLF
HHHHHHCCHHHHHHH		14.0422802335
1571UbiquitinationKSHNIVQKTALNWRL
HHCCHHHHHHHHHHH		25.52-
1579PhosphorylationTALNWRLSARNAARR
HHHHHHHHHHHHHHH		19.3327600695
1588PhosphorylationRNAARRDSVLAASRD
HHHHHHHHHHHHCHH		19.7424925903
1593PhosphorylationRDSVLAASRDYRNII
HHHHHHHCHHHHHHH		21.7828833060
1639 (in isoform 2)Ubiquitination-43.42-
1645 (in isoform 2)Ubiquitination-36.48-
1654UbiquitinationESGGFICKLIKHTKQ
HHCCHHHHHHHHHHH		48.7222790023
1654 (in isoform 2)Ubiquitination-48.7222790023
1658 (in isoform 2)Ubiquitination-31.16-
1660UbiquitinationCKLIKHTKQLLEENE
HHHHHHHHHHHHHCH		38.3722790023
1660 (in isoform 2)Ubiquitination-38.3722790023
1673UbiquitinationNEEKLCIKVLQTLRE
CHHHHHHHHHHHHHH		35.5822790023
1673 (in isoform 2)Ubiquitination-35.5822790023
1750PhosphorylationYYGNIRPSGRRESLT
HCCCCCCCCCCCCCC		34.7729472430
1755PhosphorylationRPSGRRESLTSFGNG
CCCCCCCCCCCCCCC		34.8325521595
1757PhosphorylationSGRRESLTSFGNGPL
CCCCCCCCCCCCCCC		31.1524925903
1758PhosphorylationGRRESLTSFGNGPLS
CCCCCCCCCCCCCCC		36.1325619855
1765PhosphorylationSFGNGPLSPGGPSKP
CCCCCCCCCCCCCCC		25.3226239621
1770PhosphorylationPLSPGGPSKPGGGGG
CCCCCCCCCCCCCCC		55.5526239621
1771UbiquitinationLSPGGPSKPGGGGGG
CCCCCCCCCCCCCCC		51.30-
1781PhosphorylationGGGGGPGSSSTSRGE
CCCCCCCCCCCCCCC		25.0125619855
1782PhosphorylationGGGGPGSSSTSRGEM
CCCCCCCCCCCCCCC		43.4825619855
1783PhosphorylationGGGPGSSSTSRGEMS
CCCCCCCCCCCCCCC		31.9025619855
1784PhosphorylationGGPGSSSTSRGEMSL
CCCCCCCCCCCCCCC		25.1325619855
1785PhosphorylationGPGSSSTSRGEMSLA
CCCCCCCCCCCCCCE		39.9925619855
1823PhosphorylationSDRVFHESILLAIAL
CCCHHHHHHHHHHHH		15.2329899451
1837PhosphorylationLLEGGNTTIQHSFFC
HHHCCCCEEEECEEE		23.7329899451
1842 (in isoform 2)Ubiquitination-6.68-
1857UbiquitinationKKSEKFFKVFYDRMK
CCCHHHHHHHHHHHH		34.2722790023
1857 (in isoform 2)Ubiquitination-34.2722790023
1884UbiquitinationNTSDLGNKKKDDEVD
CHHHCCCCCCCCCCC		60.44-
1885UbiquitinationTSDLGNKKKDDEVDR
HHHCCCCCCCCCCCC		66.49-
1886UbiquitinationSDLGNKKKDDEVDRD
HHCCCCCCCCCCCCC		72.52-
1899UbiquitinationRDAPSRKKAKEPTTQ
CCCCCHHHCCCCCHH		64.68-
1901UbiquitinationAPSRKKAKEPTTQIT
CCCHHHCCCCCHHHC		73.44-
1919PhosphorylationRDQLLEASAATRKAF
HHHHHHHHHHHHHHH		14.7321454597
1924UbiquitinationEASAATRKAFTTFRR
HHHHHHHHHHHHHHH		43.42-
1941PhosphorylationDPDDHYQSGEGTQAT
CCCCCCCCCCCCCCC		31.4823684622
2056PhosphorylationENQNCIATHESNGID
CCCCCEECCCCCCCC		13.28-
2092PhosphorylationLELKNNASKLLLAIM
HHHCCCHHHHHHHHH		26.4220531401
2103 (in isoform 2)Ubiquitination-52.83-
2118UbiquitinationILYNMRPKELVEVIK
HHHHCCHHHHHHHHH		54.0022790023
2118 (in isoform 2)Ubiquitination-54.0022790023
2152 (in isoform 2)Ubiquitination-16.21-
2167UbiquitinationHQLARHNKELQTMLK
HHHHHCCHHHHHHCC		54.3922790023
2167 (in isoform 2)Ubiquitination-54.3922790023
2223 (in isoform 2)Ubiquitination-42.76-
2238UbiquitinationERDEQGSKINDFFLR
CCCCCCCCCCCCHHC		52.9722790023
2238 (in isoform 2)Ubiquitination-52.9722790023
2242 (in isoform 2)Ubiquitination-5.55-
2257UbiquitinationFNEMNWQKKLRAQPV
HHHCCHHHHHCHHHH		45.4422790023
2257 (in isoform 2)Ubiquitination-45.4422790023
2655PhosphorylationKVKDSTEYTGPESYV
ECCCCCCCCCCHHHH		19.65-
2681PhosphorylationFPRMRAMSLVSSDSE
HHHHHHHHHHCCCCH		25.3219060867
2684PhosphorylationMRAMSLVSSDSEGEQ
HHHHHHHCCCCHHHH		33.4529899451
2685PhosphorylationRAMSLVSSDSEGEQN
HHHHHHCCCCHHHHH		37.3629899451
2685 (in isoform 2)Ubiquitination-37.36-
2687PhosphorylationMSLVSSDSEGEQNEL
HHHHCCCCHHHHHHH		49.8329472430
2691 (in isoform 2)Ubiquitination-60.60-
2700UbiquitinationELRNLQEKLESTMKL
HHHHHHHHHHHHHHH		44.5922790023
2700 (in isoform 2)Ubiquitination-44.5922790023
2703PhosphorylationNLQEKLESTMKLVTN
HHHHHHHHHHHHHHH		44.2126239621
2704PhosphorylationLQEKLESTMKLVTNL
HHHHHHHHHHHHHHH		14.6726239621
2706UbiquitinationEKLESTMKLVTNLSG
HHHHHHHHHHHHHHH		39.6422790023
2706 (in isoform 2)Ubiquitination-39.6422790023
2709PhosphorylationESTMKLVTNLSGQLS
HHHHHHHHHHHHHHH		40.6626239621
2712PhosphorylationMKLVTNLSGQLSELK
HHHHHHHHHHHHHHH		26.9426239621
2723PhosphorylationSELKDQMTEQRKQKQ
HHHHHHHHHHHHHHH		24.2722871156
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
421SPhosphorylationKinaseCDK1P06493
PSP
421SPhosphorylationKinaseCDK1P11440
PhosphoELM
436SPhosphorylationKinaseMK01P63085
PhosphoELM
436SPhosphorylationKinaseMAPK1P28482
GPS
799TPhosphorylationKinaseCDK1P06493
PSP
799TPhosphorylationKinaseCDK1P11440
PhosphoELM
1588SPhosphorylationKinasePRKACAP17612
GPS
1588SPhosphorylationKinaseKAPCAP05132
PhosphoELM
1588SPhosphorylationKinasePKA-FAMILY-GPS
1588SPhosphorylationKinasePKG-FAMILY-GPS
1755SPhosphorylationKinaseKAPCAP05132
PhosphoELM
1755SPhosphorylationKinasePRKACAP17612
GPS
1755SPhosphorylationKinasePKA-FAMILY-GPS
1755SPhosphorylationKinasePKA-Uniprot
1765SPhosphorylationKinaseMAPK1P28482
GPS
1765SPhosphorylationKinaseMK01P63085
PhosphoELM
2656TPhosphorylationKinasePLK1Q07832
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

-
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ITPR1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RN170_MOUSERnf170physical
21610068
TERA_MOUSEVcpphysical
21610068
ERLN2_MOUSEErlin2physical
21610068
TERA_MOUSEVcpphysical
16103111
UFD1_MOUSEUfd1lphysical
16103111
UBE4B_MOUSEUbe4bphysical
16103111
NPL4_MOUSENploc4physical
16103111
GRM1_MOUSEGrm1physical
15579147
ITPR1_MOUSEItpr1physical
15579147
HOME1_MOUSEHomer1physical
15579147
GRID2_MOUSEGrid2physical
15579147
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITPR1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASSSPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASSSPECTROMETRY.

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