dbPTM

PLCL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLCL1_MOUSE
UniProt AC	Q3USB7
Protein Name	Inactive phospholipase C-like protein 1
Gene Name	Plcl1
Organism	Mus musculus (Mouse).
Sequence Length	1096
Subcellular Localization	Cytoplasm.
Protein Description	Involved in an inositol phospholipid-based intracellular signaling cascade. Shows no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. Component in the phospho-dependent endocytosis process of GABA A receptor. Acts as a inhibitor of PPP1C (By similarity). Involved in the assembly and/or the trafficking of gamma-2 subunit-containing GABA A receptors..
Protein Sequence	MAEGAASREAPAPLDVAGGEDDPRAGADAASGDAPPPALGGRMRDRRSGVALPGAAGVPADSEAGLLEAARATPRRSSIIKDPSNQKCGGRKKTVSFSSMPSEKKISSAHDCISFMQAGCELKKVRPNSRIYNRFFTLDTDLQALRWEPSKKDLEKAKLDISAIKEIRLGKNTETFRNNGLADQICEDCAFSILHGENYESLDLVANSADVANIWVSGLRYLVSRSKQPLDFIEGNQNTPRFMWLKTVFEAADVDGNGIMLEDTSVELIKQLNPTLKESKIRLKFKEIQKSKEKLTTRVTEEEFCEAFCELCTRPEVYFLLVQISKNKEYLDANDLMLFLEAEQGVTHITEDMCLDIIRRYELSEDGRQKGFLAIDGFTQYLLSPECDIFDPEQKKVAQDMTQPLSHYYINASHNTYLIEDQFRGPADINGYVRALKMGCRSIELDVSDGPDNEPILCNRNNMAMHLSFRSVLEVINKFAFVASEYPLILCLGNHCSLPQQKVMAQQMKKVFGEKLYTEAPLSSESYLPSPEKLKNMIIVKGKKLPSESDLLEGEVTDEDEEAEMSRRMSGDYNGEQKHIWLCRELSDLVSICKSVQHRDFELSMKTQNYWEMCSFSETEASRIANEYPEDFVNYNKKFLSRVYPSAMRIDSSNLNPQDFWNCGCQIVAMNFQTPGPMMDLHTGWFLQNGGCGYVLRPSIMRDEVSYFSANTKGIVPGVSPLVLHIKIISGQNFPKPKGACAKGDVIDPYVCVEIHGIPADCCEQRTKTVQQNSDNPIFDETFEFQVNLPELTMVRFVILDDDYIGDEFIGQYTIPFECLQPGYRHVPLRSFVGDIMEHVTLFVHIAITNRSGGGKPQKRSLSVRMGKKVREYTMLRNIGLKTIDDIFKIAVHPLREAIDMRENMQNAIVSVKELCGLPPIASLKQCLLTLSSRLITSDSTPSVSLVMKDCFPYLEPLGAIPDVQKRMLAAYDLMIQESRVLIEMADTVQEKIVQCQKAGMEFHEELHNLGAKEGLKGRKLNKAIESFAWNITVLKGQGDLLKNAKNEAVENIKQIQLACLSCGLSKGPGGGSEAKGKRSLEAIEEKESSEENGKL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	Phosphorylation	GRMRDRRSGVALPGA CCCCCCCCCCCCCCC	38.21	27180971
62	Phosphorylation	AAGVPADSEAGLLEA CCCCCCCCHHHHHHH	31.30	24719451
73	Phosphorylation	LLEAARATPRRSSII HHHHHHHCCCCHHCC	16.27	23527152
77	Phosphorylation	ARATPRRSSIIKDPS HHHCCCCHHCCCCCC	27.45	26060331
78	Phosphorylation	RATPRRSSIIKDPSN HHCCCCHHCCCCCCC	26.90	26824392
94	Phosphorylation	KCGGRKKTVSFSSMP CCCCCCCEEECCCCC	25.15	25521595
96	Phosphorylation	GGRKKTVSFSSMPSE CCCCCEEECCCCCCC	25.33	25521595
98	Phosphorylation	RKKTVSFSSMPSEKK CCCEEECCCCCCCCC	20.44	22324799
99	Phosphorylation	KKTVSFSSMPSEKKI CCEEECCCCCCCCCC	32.47	22324799
102	Phosphorylation	VSFSSMPSEKKISSA EECCCCCCCCCCCCH	54.10	28833060
277	Ubiquitination	KQLNPTLKESKIRLK HHHCCCCCHHHHHHH	63.52	27667366
533	Ubiquitination	SYLPSPEKLKNMIIV CCCCCHHHHCCEEEE	69.05	22790023
547	Phosphorylation	VKGKKLPSESDLLEG ECCCCCCCHHHCCCC	61.23	-
549	Phosphorylation	GKKLPSESDLLEGEV CCCCCCHHHCCCCCC	37.59	24925903
557	Phosphorylation	DLLEGEVTDEDEEAE HCCCCCCCCHHHHHH	29.39	25521595
566	Phosphorylation	EDEEAEMSRRMSGDY HHHHHHHHHHHCCCC	14.29	25293948
570	Phosphorylation	AEMSRRMSGDYNGEQ HHHHHHHCCCCCCCH	27.05	25521595
573	Phosphorylation	SRRMSGDYNGEQKHI HHHHCCCCCCCHHEE	28.70	29899451
637	Ubiquitination	EDFVNYNKKFLSRVY HHHHCCCHHHHHHHC	34.24	27667366
641	Phosphorylation	NYNKKFLSRVYPSAM CCCHHHHHHHCCCCE	23.88	23737553
644	Phosphorylation	KKFLSRVYPSAMRID HHHHHHHCCCCEECC	7.14	23737553
646	Phosphorylation	FLSRVYPSAMRIDSS HHHHHCCCCEECCCC	19.60	23737553
861	Phosphorylation	GGKPQKRSLSVRMGK CCCCCCCCCHHHCCH	31.84	23737553
863	Phosphorylation	KPQKRSLSVRMGKKV CCCCCCCHHHCCHHH	14.66	23737553
966	Ubiquitination	GAIPDVQKRMLAAYD CCCCHHHHHHHHHHH	39.36	-
1060	S-palmitoylation	IKQIQLACLSCGLSK HHHHHHHHHHCCCCC	3.80	28680068
1080	Phosphorylation	SEAKGKRSLEAIEEK CHHHCHHHHHHHHHH	33.76	25521595

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
94	T	Phosphorylation	Kinase	PRKACA	P05132	GPS
94	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
94	T	Phosphorylation	Kinase	PKA	-	Uniprot
96	S	Phosphorylation	Kinase	PRKACA	P05132	GPS
96	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
96	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
94	T	Phosphorylation		15306641
Phosphorylation of Thr-94 resulted in dissociation of PPP1C from PRIP1.

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 PLCL1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PLCL1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PLCL1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-557, AND MASSSPECTROMETRY.	19367708 [Abstract]
"GABAA receptor phospho-dependent modulation is regulated byphospholipase C-related inactive protein type 1, a novel proteinphosphatase 1 anchoring protein."; Terunuma M., Jang I.S., Ha S.H., Kittler J.T., Kanematsu T.,Jovanovic J.N., Nakayama K.I., Akaike N., Ryu S.H., Moss S.J.,Hirata M.; J. Neurosci. 24:7074-7084(2004). Cited for: PHOSPHORYLATION AT THR-94, AND MUTAGENESIS OF THR-94.	15306641 [Abstract]

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