dbPTM

PLCB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLCB1_HUMAN
UniProt AC	Q9NQ66
Protein Name	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
Gene Name	PLCB1
Organism	Homo sapiens (Human).
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	MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSSEELGGDIPGKEFDTPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	S-palmitoylation	ALQLKPVCVSDSLKK EEEEECEEEECHHCC	3.08	-
26	Phosphorylation	SDSLKKGTKFVKWDD ECHHCCCCCEEECCC	30.13	-
39	Phosphorylation	DDDSTIVTPIILRTD CCCCCEEEEEEEEEC	12.62	24076635
67	Phosphorylation	ETELLDLSLVKDARC CEEEEEHHHHCCCCC	30.68	24505115
70	Ubiquitination	LLDLSLVKDARCGRH EEEHHHHCCCCCCCC	51.46	29967540
136	Phosphorylation	EWTNEVFSLATNLLA HHHHHHHHHHHHHHH	23.44	-
139	Phosphorylation	NEVFSLATNLLAQNM HHHHHHHHHHHHHHC	31.52	-
160	Ubiquitination	EKAYTKLKLQVTPEG HHHHHHHHEECCCCC	38.13	30230243
172	Malonylation	PEGRIPLKNIYRLFS CCCCCCHHHHHHHHH	35.62	26320211
187	O-linked_Glycosylation	ADRKRVETALEACSL CCHHHHHHHHHHCCC	33.41	30379171
236	Phosphorylation	FSEFGAKSKPYLTVD HHHHCCCCCCEEEHH	38.03	-
239	Phosphorylation	FGAKSKPYLTVDQMM HCCCCCCEEEHHHHH	20.81	22817900
278	Phosphorylation	VQVLIEKYEPNNSLA HHHHHHHCCCCCHHH	24.67	30576142
355	Phosphorylation	MYRQVLLSGCRCVEL HHHHHHHHCCEEEEE	31.52	29083192
387	Phosphorylation	FTMTTEISFKEVIEA EEEEEEECHHHHHHH	24.84	24719451
410	Phosphorylation	SPFPILLSFENHVDS CCCCEEEEEECCCCC	27.37	28348404
417	Phosphorylation	SFENHVDSPKQQAKM EEECCCCCHHHHHHH	32.67	24076635
423	Ubiquitination	DSPKQQAKMAEYCRL CCHHHHHHHHHHHHH	34.01	-
444	Phosphorylation	LMEPLEKYPLESGVP HCCCHHHCCCCCCCC	12.04	-
448	Phosphorylation	LEKYPLESGVPLPSP HHHCCCCCCCCCCCH	53.42	-
454	Phosphorylation	ESGVPLPSPMDLMYK CCCCCCCCHHHHHHH	40.31	29978859
460	Phosphorylation	PSPMDLMYKILVKNK CCHHHHHHHHHHHCC	11.37	29978859
473	O-linked_Glycosylation	NKKKSHKSSEGSGKK CCCCCCCCCCCCCCH	28.35	30379171
500	Phosphorylation	SSSMFEPSSPGAGEA CCCCCCCCCCCCCCC	41.80	23898821
501	Phosphorylation	SSMFEPSSPGAGEAD CCCCCCCCCCCCCCC	37.76	23898821
509	Phosphorylation	PGAGEADTESDDDDD CCCCCCCCCCCCCCC	44.42	27251275
511	Phosphorylation	AGEADTESDDDDDDD CCCCCCCCCCCCCCC	48.72	27251275
524	Phosphorylation	DDDCKKSSMDEGTAG CCCHHHHHCCCCCCC	38.85	-
558	Phosphorylation	KFESFEISKKRNKSF EECCEEEECCCCCCC	25.56	-
569	Phosphorylation	NKSFEMSSFVETKGL CCCCCCHHHHECCCH	31.81	17924679
573	Phosphorylation	EMSSFVETKGLEQLT CCHHHHECCCHHHHH	25.72	17924679
582	Phosphorylation	GLEQLTKSPVEFVEY CHHHHHCCCCCHHHH	29.01	24076635
735	Ubiquitination	EEEPIVFKKVVLPTL CCCCCCEEECHHHHH	33.49	29967540
798	Phosphorylation	VYIEVKDYVPDTYAD EEEEEHHHCCCCHHH	14.25	29116813
802	Phosphorylation	VKDYVPDTYADVIEA EHHHCCCCHHHHHHH	17.97	28796482
803	Phosphorylation	KDYVPDTYADVIEAL HHHCCCCHHHHHHHH	14.26	28796482
816	Phosphorylation	ALSNPIRYVNLMEQR HHHCHHHHHHHHHHH	8.39	28796482
867	Phosphorylation	AENGVNHTTTLTPKP CCCCCCCCCCCCCCC	19.10	27251275
868	Phosphorylation	ENGVNHTTTLTPKPP CCCCCCCCCCCCCCC	16.56	28348404
869	Phosphorylation	NGVNHTTTLTPKPPS CCCCCCCCCCCCCCH	29.77	28348404
871	Phosphorylation	VNHTTTLTPKPPSQA CCCCCCCCCCCCHHH	27.46	28348404
876	Phosphorylation	TLTPKPPSQALHSQP CCCCCCCHHHCCCCC	36.29	28348404
881	Phosphorylation	PPSQALHSQPAPGSV CCHHHCCCCCCCCCC	38.41	28348404
887	Phosphorylation	HSQPAPGSVKAPAKT CCCCCCCCCCCCCCH	21.27	11278470
918	Phosphorylation	EELKQQKSFVKLQKK HHHHHHHHHHHHHHH	30.82	22817900
941	Phosphorylation	VKRHHKKTTDLIKEH HHHHHHHHHHHHHHH	30.28	30622161
942	Phosphorylation	KRHHKKTTDLIKEHT HHHHHHHHHHHHHHH	37.37	30622161
952	Phosphorylation	IKEHTTKYNEIQNDY HHHHHHHHHHHHHHH	18.88	23403867
959	Phosphorylation	YNEIQNDYLRRRAAL HHHHHHHHHHHHHHH	15.06	23403867
969	Phosphorylation	RRAALEKSAKKDSKK HHHHHHHHHCCCCCC	35.63	24173317
971	Acetylation	AALEKSAKKDSKKKS HHHHHHHCCCCCCCC	65.29	19666589
972	Acetylation	ALEKSAKKDSKKKSE HHHHHHCCCCCCCCC	67.93	89459
976	Acetylation	SAKKDSKKKSEPSSP HHCCCCCCCCCCCCC	66.54	89461
978	Phosphorylation	KKDSKKKSEPSSPDH CCCCCCCCCCCCCCC	64.72	18510355
981	Phosphorylation	SKKKSEPSSPDHGSS CCCCCCCCCCCCCCC	50.91	29116813
982	Phosphorylation	KKKSEPSSPDHGSST CCCCCCCCCCCCCCH	45.09	29116813
987	Phosphorylation	PSSPDHGSSTIEQDL CCCCCCCCCHHHHHH	22.38	18510355
988	Phosphorylation	SSPDHGSSTIEQDLA CCCCCCCCHHHHHHH	37.69	18510355
989	Phosphorylation	SPDHGSSTIEQDLAA CCCCCCCHHHHHHHH	30.17	28857561
1024	Phosphorylation	LNLRQEQYYSEKYQK HHHHHHHHHHHHHHH	14.27	-
1025	Phosphorylation	NLRQEQYYSEKYQKR HHHHHHHHHHHHHHH	15.28	-
1026	Phosphorylation	LRQEQYYSEKYQKRE HHHHHHHHHHHHHHH	23.76	-
1074	Acetylation	ELKKKMDKKRQEKIT HHHHHHHHHHHHHHH	46.48	88455
1075	Acetylation	LKKKMDKKRQEKITE HHHHHHHHHHHHHHH	55.86	18527913
1085	Phosphorylation	EKITEAKSKDKSQME HHHHHHHHCCHHHHH	53.81	29759185
1089	Phosphorylation	EAKSKDKSQMEEEKT HHHHCCHHHHHHHHH	44.91	29759185
1102	Phosphorylation	KTEMIRSYIQEVVQY HHHHHHHHHHHHHHH	9.22	-
1109	Phosphorylation	YIQEVVQYIKRLEEA HHHHHHHHHHHHHHH	9.22	22817900
1145 (in isoform 2)	Phosphorylation	-	33.36	26471730
1146 (in isoform 2)	Phosphorylation	-	9.64	26471730
1147	Phosphorylation	PKLQVELEQEYQDKF CCHHHHHHHHHHHHH	28.06	27251275
1147 (in isoform 2)	Phosphorylation	-	28.06	26471730
1150 (in isoform 2)	Phosphorylation	-	23.00	27251275
1152 (in isoform 2)	Phosphorylation	-	58.41	27251275
1158 (in isoform 2)	Phosphorylation	-	31.79	27251275
1160 (in isoform 2)	Phosphorylation	-	43.52	28348404
1164 (in isoform 2)	Phosphorylation	-	6.52	28348404
1177	Phosphorylation	KGKISEDSNHGSAPL CCCCCCCCCCCCCCC	27.03	25307156
1197	Phosphorylation	PGKVNHKTPSSEELG CCCCCCCCCCHHHCC	22.35	23403867
1199	Phosphorylation	KVNHKTPSSEELGGD CCCCCCCCHHHCCCC	56.46	23898821
1200	Phosphorylation	VNHKTPSSEELGGDI CCCCCCCHHHCCCCC	35.97	28348404

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-FAMILY	-	GPS
887	S	Phosphorylation	Kinase	PKC	-	Uniprot
887	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
982	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
982	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

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

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRPM7_HUMAN	TRPM7	physical	11941371
SPTB2_HUMAN	SPTBN1	physical	20936779
GNA11_HUMAN	GNA11	physical	12193606
NHRF1_HUMAN	SLC9A3R1	physical	12193606
GNAQ_HUMAN	GNAQ	physical	11753430
PLCB1_HUMAN	PLCB1	physical	11753430
CEP76_HUMAN	CEP76	physical	25416956
GNAQ_HUMAN	GNAQ	physical	16754659

Drug and Disease Associations

Kegg Disease
H00606	Early infantile epileptic encephalopathy; Ohtahara syndrome
OMIM Disease
613722	Epileptic encephalopathy, early infantile, 12 (EIEE12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PLCB1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-972 AND LYS-976, AND MASSSPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND THR-573, ANDMASS SPECTROMETRY.	17924679 [Abstract]

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