dbPTM

ITPR1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ITPR1_RAT
UniProt AC	P29994
Protein Name	Inositol 1,4,5-trisphosphate receptor type 1
Gene Name	Itpr1
Organism	Rattus norvegicus (Rat).
Sequence Length	2750
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 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	MSDKMSSFLHIGDICSLYAEGSTNGFISTLGLVDDRCVVQPEAGDLNNPPKKFRDCLFKLCPMNRYSAQKQFWKAAKPGANSTTDAVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSHQLVDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEVDPDFEEECLEFQPSVDPDQDASRSRLRNAQEKMVYSLVSVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNIPIDKEEEKPVMLKIGTSPLKEDKEAFAIVPVSPAEVRDLDFANDASKVLGSIAGKLEKGTITQNERRSVTKLLEDLVYFVTGGTNSGQDVLEVVFSKPNRERQKLMREQNILKQIFKLLQAPFTDCGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPTNADILIETKLVLSRFEFEGVSTGENALEAGEDEEEVWLFWRDSNKEIRSKSVRELAQDAKEGQKEDRDVLSYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPYDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGASKDEIKERFAQTMEFVEEYLRDVVCQRFPFSDKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAILDCVHVTTIFPISKMTKGEENKGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAAPEGNVKQAEPEKEDIMVMDTKLKIIEILQFILNVRLDYRISCLLCIFKREFDESNSQSSETSSGNSSQEGPSNVPGALDFEHIEEQAEGIFGGSEENTPLDLDDHGGRTFLRVLLHLTMHDYPPLVSGALQLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGQGPDEPMDGASGENEHKKTEEGTSKPLKHESTSSYNYRVVKEILIRLSKLCVQESASVRKSRKQQQRLLRNMGAHAVVLELLQIPYEKAEDTKMQEIMRLAHEFLQNFCAGNQQNQALLHKHINLFLNPGILEAVTMQHIFMNNFQLCSEINERVVQHFVHCIETHGRNVQYIKFLQTIVKAEGKFIKKCQDMVMAELVNSGEDVLVFYNDRASFQTLIQMMRSERDRMDENSPLFMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCIPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRACNNTSDRKHADSVLEKYVTEIVMSIVTTFFSSPFSDQSTTLQTRQPVFVQLLQGVFRVYHCNWLMPSQKASVESCIRVLSDVAKSRAIAIPVDLDSQVNNLFLKSHNIVQKTAMNWRLSARNAARRDSVLAASRDYRNIIERLQDIVSALEDRLRPLVQAELSVLVDVLHRPELLFPENTDARRKCESGGFICKLIKHTKQLLEENEEKLCIKVLQTLREMMTKDRGYGEKQISIDELENAELPQPPEAENSTEQELEPSPPLRQLEDHKRGEALRQILVNRYYGNIRPSGRRESLTSFGNGPLSPGGPSKPGGGGGGPGSGSTSRGEMSLAEVQCHLDKEGASNLVIDLIMNASSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFYDRMKVAQQEIKATVTVNTSDLGNKKKDDEVDRDAPSRKKAKEPTTQITEEVRDQLLEASAATRKAFTTFRREADPDDHYQSGEGTQATTDKAKDDLEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKTNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGKKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYMQGEVEFEDGENGEDGAASPRNVGHNIYILAHQLARHNKELQTMLKPGGQVDGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKINDFFLRSEDLFNEMNWQKKLRAQPVLYWCARNMSFWSSISFNLAVLMNLLVAFFYPFKGVRGGTLEPHWSGLLWTAMLISLAIVIALPKPHGIRALIASTILRLIFSVGLQPTLFLLGAFNVCNKIIFLMSFVGNCGTFTRGYRAMVLDVEFLYHLLYLLICAMGLFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRPIILTAALALILVYLFSIVGYLFFKDDFILEVDRLPNETAGPETGESLANDFLYSDVCRVETGENCTSPAPKEELLPVEETEQDKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEILKTTCFICGLERDKFDNKTVTFEEHIKEEHNMWHYLCFIVLVKVKDSTEYTGPESYVAEMIRERNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMKLVTNLSGQLSELKDQMTEQRKQKQRIGLLGHPPHMNVNPQQPA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
56	S-palmitoylation	PPKKFRDCLFKLCPM CCHHHHHHHHHHCCC	4.13	25368151
91	Acetylation	TDAVLLNKLHHAADL HHHHHHHHHHHHHHH	49.52	22902405
100	Acetylation	HHAADLEKKQNETEN HHHHHHHHHCCHHHH	67.94	22902405
230	Acetylation	FMKWSDNKDDILKGG EEEECCCHHHHCCCC	62.86	22902405
421	Phosphorylation	VMLKIGTSPLKEDKE CEEEEECCCCCCCCC	24.03	16237118
424	Ubiquitination	KIGTSPLKEDKEAFA EEECCCCCCCCCEEE	68.22	-
436	Phosphorylation	AFAIVPVSPAEVRDL EEEEEECCHHHHCCC	16.60	23984901
450	Phosphorylation	LDFANDASKVLGSIA CCCCCCHHHHHHHHH	26.59	23984901
459	Acetylation	VLGSIAGKLEKGTIT HHHHHHHHCCCCCCC	44.44	22902405
462	Acetylation	SIAGKLEKGTITQNE HHHHHCCCCCCCHHH	72.32	22902405
482	Phosphorylation	KLLEDLVYFVTGGTN HHHHHHCHHHHCCCC	10.30	-
517	Acetylation	MREQNILKQIFKLLQ HHHHHHHHHHHHHHH	37.23	22902405
576	Acetylation	KNQEYIAKQFGFMQK HCHHHHHHHHCCCHH	36.28	22902405
799	Phosphorylation	RDPQEQVTPVKYARL CCHHHCCCCCHHHHH	23.27	16237118
849	S-palmitoylation	EYLRDVVCQRFPFSD HHHHHHHHHHCCCCH	2.11	25368151
916	Ubiquitination	MTKGEENKGSNVMRS CCCCCCCCCCCHHHH	67.98	18955483
945	Phosphorylation	GGGFLPMTPMAAAPE CCCCCCCCCCCCCCC	14.15	-
962	Ubiquitination	VKQAEPEKEDIMVMD CCCCCCCHHCCEEEC	71.98	18955483
971	Acetylation	DIMVMDTKLKIIEIL CCEEECCHHHHHHHH	43.44	22902405
1116	Acetylation	VDNYKQIKQDLDQLR CCCHHHHHHHHHHHH	34.95	22902405
1572	Ubiquitination	KSHNIVQKTAMNWRL HHCCHHHHHHHHHHH	27.62	18955483
1589	Phosphorylation	RNAARRDSVLAASRD HHHHHHHHHHHHCHH	19.74	23712012
1756	Phosphorylation	RPSGRRESLTSFGNG CCCCCCCCCCCCCCC	34.83	23712012
1758	Phosphorylation	SGRRESLTSFGNGPL CCCCCCCCCCCCCCC	31.15	27097102
1759	Phosphorylation	GRRESLTSFGNGPLS CCCCCCCCCCCCCCC	36.13	27097102
1766	Phosphorylation	SFGNGPLSPGGPSKP CCCCCCCCCCCCCCC	25.32	23984901
1771	Phosphorylation	PLSPGGPSKPGGGGG CCCCCCCCCCCCCCC	55.55	25575281
1772	Ubiquitination	LSPGGPSKPGGGGGG CCCCCCCCCCCCCCC	51.30	18955483
1885	Ubiquitination	NTSDLGNKKKDDEVD CHHHCCCCCCCCCCC	60.44	18955483
1886	Ubiquitination	TSDLGNKKKDDEVDR HHHCCCCCCCCCCCC	66.49	18955483
1887	Ubiquitination	SDLGNKKKDDEVDRD HHCCCCCCCCCCCCC	72.52	18955483
1902	Ubiquitination	APSRKKAKEPTTQIT CCCHHHCCCCCHHHC	73.44	18955483
1925	Ubiquitination	EASAATRKAFTTFRR HHHHHHHHHHHHHHH	43.42	18955483
2119	Ubiquitination	ILYNMRPKELVEVIK HHHHCCHHHHHHHHH	54.00	18955483
2126	Acetylation	KELVEVIKKAYMQGE HHHHHHHHHHHHCCC	36.20	22902405
2258	Ubiquitination	FNEMNWQKKLRAQPV HHHCCHHHHHCHHHH	45.44	18955483
2656	Phosphorylation	KVKDSTEYTGPESYV ECCCCCCCCCCHHHH	19.65	-
2682	Phosphorylation	FPRMRAMSLVSSDSE HHHHHHHHHHCCCCH	25.32	16332683
2685	Phosphorylation	MRAMSLVSSDSEGEQ HHHHHHHCCCCHHHH	33.45	28432305
2686	Phosphorylation	RAMSLVSSDSEGEQN HHHHHHCCCCHHHHH	37.36	28432305
2688	Phosphorylation	MSLVSSDSEGEQNEL HHHHCCCCHHHHHHH	49.83	28432305

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
310	T	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
1589	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
1589	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
1589	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
1589	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
1756	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
1756	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
1756	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
1756	S	Phosphorylation	Kinase	PKG-FAMILY	-	GPS
1756	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
1756	S	Phosphorylation	Kinase	PKG/CGK_GROUP	-	PhosphoELM
2682	S	Phosphorylation	Kinase	AKT1	P31749	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
48	K	ubiquitylation		18955483
Approximately 40% of the ITPR1-associated ubiquitin is monoubiquitin, and polyubiquitins are both 'Lys-48'- and 'Lys-63'-linked.

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBC_RAT	Ubc	physical	10191279
UBC_RAT	Ubc	physical	21071436
TERA_RAT	Vcp	physical	16103111
UFD1_RAT	Ufd1l	physical	16103111
UBE4A_RAT	Ube4a	physical	16103111
ERLN2_RAT	Erlin2	physical	17502376
NAC1_RAT	Slc8a1	physical	14593108
AT1A3_RAT	Atp1a3	physical	14593108
SPTN1_RAT	Sptan1	physical	14593108

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ITPR1_RAT

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"Mass spectrometric analysis of type 1 inositol 1,4,5-trisphosphatereceptor 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). 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.	18955483 [Abstract]

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