dbPTM

PLCB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLCB1_MOUSE
UniProt AC	Q9Z1B3
Protein Name	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
Gene Name	Plcb1
Organism	Mus musculus (Mouse).
Sequence Length	1216
Subcellular Localization	Nucleus membrane . Cytoplasm. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes..
Protein Description	The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes..
Protein Sequence	MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKAPKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTASLAPKPPSQAPHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHNEIRQQILDEKPKLQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPPSLASDAAKVNLKSPSSEEIERENPGREFDTPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	S-palmitoylation	ALQLKPVCVSDSLKK EEEEECEEEECHHCC	3.08	27653213
30	Ubiquitination	KKGTKFVKWDDDSTI CCCCCEEECCCCCCE	48.30	22790023
160	Ubiquitination	EKAYTKLKLQVTPEG HHHHHHHHEECCCCC	38.13	22790023
164	Phosphorylation	TKLKLQVTPEGRIPL HHHHEECCCCCCCCH	11.58	-
179	Phosphorylation	KNIYRLFSADRKRVE HHHHHHHHCCHHHHH	33.57	21743459
220	S-palmitoylation	RVFLNNLCPRPEIDN HHHHHCCCCCHHHHC	2.67	28680068
236	Phosphorylation	FSEFGAKSKPYLTVD HHHHCCCCCCEEEHH	38.03	22817900
239	Phosphorylation	FGAKSKPYLTVDQMM HCCCCCCEEEHHHHH	20.81	22807455
333	Phosphorylation	FINSSHNTYLTAGQL HCCCCCCCEEEHHHC	17.93	15572359
334	Phosphorylation	INSSHNTYLTAGQLA CCCCCCCEEEHHHCC	13.84	15572359
336	Phosphorylation	SSHNTYLTAGQLAGN CCCCCEEEHHHCCCC	20.51	15572359
410	Phosphorylation	SPFPILLSFENHVDS CCCCEEEEEECCCCC	27.37	22324799
417	Phosphorylation	SFENHVDSPKQQAKM EEECCCCCHHHHHHH	32.67	22324799
501	Phosphorylation	SSVFEPSSPGAGEAD CCCCCCCCCCCCCCC	37.76	29899451
509	Phosphorylation	PGAGEADTESDDDDD CCCCCCCCCCCCCCC	44.42	22817900
511	Phosphorylation	AGEADTESDDDDDDD CCCCCCCCCCCCCCC	48.72	22817900
523	Phosphorylation	DDDDCKKSSMDEGTA CCCCHHHHHCCCCCC	19.18	29899451
554	Phosphorylation	IQPVKFESFEISKKR HHCCEECCEEEECCC	31.17	25521595
564	Phosphorylation	ISKKRNKSFEMSSFV EECCCCCCCCCHHHH	29.95	29899451
568	Phosphorylation	RNKSFEMSSFVETKG CCCCCCCHHHHECCC	17.27	25521595
569	Phosphorylation	NKSFEMSSFVETKGL CCCCCCHHHHECCCH	31.81	25521595
580	Phosphorylation	TKGLEQLTKSPVEFV CCCHHHHHCCCCCHH	29.21	29899451
581	Ubiquitination	KGLEQLTKSPVEFVE CCHHHHHCCCCCHHH	62.45	22790023
582	Phosphorylation	GLEQLTKSPVEFVEY CHHHHHCCCCCHHHH	29.01	25521595
589	Phosphorylation	SPVEFVEYNKMQLSR CCCCHHHHCCCCHHC	18.12	20415495
811	Phosphorylation	ADVIEALSNPIRYVN HHHHHHHHCHHHHHH	47.83	29899451
839	Ubiquitination	LEDEEEVKKEADPGE CCCHHHHHHHCCCCC	48.45	22790023
847	Phosphorylation	KEADPGETSSEAPSE HHCCCCCCCCCCCCC	43.39	25521595
848	Phosphorylation	EADPGETSSEAPSET HCCCCCCCCCCCCCC	23.14	25521595
849	Phosphorylation	ADPGETSSEAPSETR CCCCCCCCCCCCCCC	45.24	29899451
853	Phosphorylation	ETSSEAPSETRTTPA CCCCCCCCCCCCCCC	59.66	25521595
855	Phosphorylation	SSEAPSETRTTPAEN CCCCCCCCCCCCCCC	37.34	25521595
887	Phosphorylation	HSQPAPGSVKAPAKT CCCCCCCCCCCCCCH	21.27	25338131
978	Phosphorylation	KKDSKKKSEPSSPDH CCCCCCCCCCCCCCC	64.72	24925903
981	Phosphorylation	SKKKSEPSSPDHGSS CCCCCCCCCCCCCCH	50.91	24925903
982	Phosphorylation	KKKSEPSSPDHGSSA CCCCCCCCCCCCCHH	45.09	24925903
987	Phosphorylation	PSSPDHGSSAIEQDL CCCCCCCCHHHHHHH	17.12	24925903
988	Phosphorylation	SSPDHGSSAIEQDLA CCCCCCCHHHHHHHH	37.55	24925903
1002	Phosphorylation	AALDAEMTQKLIDLK HHHCHHHHHHHHCCC	17.66	20415495
1011	Ubiquitination	KLIDLKDKQQQQLLN HHHCCCHHHHHHHHH	48.71	22790023
1041	Ubiquitination	HIKLLIQKLTDVAEE HHHHHHHHHHHHHHH	46.49	22790023
1055	Ubiquitination	ECQNNQLKKLKEICE HHHHHHHHHHHHHHH	46.42	22790023
1109	Phosphorylation	YIQEVVQYIKRLEEA HHHHHHHHHHHHHHH	9.22	22817900
1174	Phosphorylation	EAMKGKISEDSNHGS HHHCCCCCCCCCCCC	38.55	29899451
1177	Phosphorylation	KGKISEDSNHGSAPP CCCCCCCCCCCCCCC	27.03	21082442
1181	Phosphorylation	SEDSNHGSAPPSLAS CCCCCCCCCCCCHHC	30.01	21082442
1197	Phosphorylation	AAKVNLKSPSSEEIE HHHCCCCCCCHHHHH	32.93	25521595
1199	Phosphorylation	KVNLKSPSSEEIERE HCCCCCCCHHHHHHH	58.43	25521595
1200	Phosphorylation	VNLKSPSSEEIEREN CCCCCCCHHHHHHHC	42.50	25521595
1214	Phosphorylation	NPGREFDTPL----- CCCCCCCCCC-----	31.63	22324799

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
887	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
17	C	Palmitoylation		27653213
Palmitoylation at Cys-17 by ZDHHC21 regulates the signaling activity of PLCB1 and the function of the endothelial barrier (Probable).

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 PLCB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PLCB1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PLCB1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Proteomic analysis of in vivo phosphorylated synaptic proteins."; Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.; J. Biol. Chem. 280:5972-5982(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; TYR-334 ANDTHR-336, AND MASS SPECTROMETRY.	15572359 [Abstract]

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