dbPTM

PLCG1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLCG1_HUMAN
UniProt AC	P19174
Protein Name	1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Gene Name	PLCG1
Organism	Homo sapiens (Human).
Sequence Length	1290
Subcellular Localization	Cell projection, lamellipodium. Cell projection, ruffle. Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.
Protein Description	Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration..
Protein Sequence	MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRAGERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSSSTELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGAASPCA ------CCCCCCCCC	27.86	19413330
6	Phosphorylation	--MAGAASPCANGCG --CCCCCCCCCCCCC	21.70	25159151
18	Phosphorylation	GCGPGAPSDAEVLHL CCCCCCCCHHHHHHH	49.25	26074081
33	Phosphorylation	CRSLEVGTVMTLFYS HHHCCCCCHHEEEEC	16.57	23401153
36	Phosphorylation	LEVGTVMTLFYSKKS CCCCCHHEEEECCCC	14.91	23401153
39	Phosphorylation	GTVMTLFYSKKSQRP CCHHEEEECCCCCCC	23.77	23401153
40	Phosphorylation	TVMTLFYSKKSQRPE CHHEEEECCCCCCCC	26.69	23401153
43	Phosphorylation	TLFYSKKSQRPERKT EEEECCCCCCCCCEE	34.85	23401153
54	Ubiquitination	ERKTFQVKLETRQIT CCEEEEEEEEEEEEE	29.80	-
63	O-linked_Glycosylation	ETRQITWSRGADKIE EEEEEEECCCHHCCC	16.52	29351928
68	Ubiquitination	TWSRGADKIEGAIDI EECCCHHCCCCCEEH	41.97	-
93	Phosphorylation	TSRDFDRYQEDPAFR CCCCHHHHCCCCCCC	20.35	-
159	Ubiquitination	QIERWLRKQFYSVDR HHHHHHHHHCCCCCC	42.46	-
159 (in isoform 2)	Ubiquitination	-	42.46	-
162	Phosphorylation	RWLRKQFYSVDRNRE HHHHHHCCCCCCCHH	12.80	25839225
175	Ubiquitination	REDRISAKDLKNMLS HHCCCCHHHHHHHHH	57.72	-
175 (in isoform 2)	Ubiquitination	-	57.72	-
178	Ubiquitination	RISAKDLKNMLSQVN CCCHHHHHHHHHHCC	50.90	21906983
178 (in isoform 2)	Ubiquitination	-	50.90	-
186	Phosphorylation	NMLSQVNYRVPNMRF HHHHHCCCCCCCHHH	17.71	22461510
205	Phosphorylation	LTDLEQRSGDITYGQ HHHHHHHHCCCCHHH	40.28	28787133
209	Phosphorylation	EQRSGDITYGQFAQL HHHHCCCCHHHHHHH	26.75	28787133
210	Phosphorylation	QRSGDITYGQFAQLY HHHCCCCHHHHHHHH	14.84	-
219	Phosphorylation	QFAQLYRSLMYSAQK HHHHHHHHHHHHHHH	12.16	-
226	Ubiquitination	SLMYSAQKTMDLPFL HHHHHHHHHCCCCCH	45.60	21890473
226 (in isoform 2)	Ubiquitination	-	45.60	-
236	Phosphorylation	DLPFLEASTLRAGER CCCCHHHHCCCCCCC	20.71	-
237	Phosphorylation	LPFLEASTLRAGERP CCCHHHHCCCCCCCC	27.58	-
304	Phosphorylation	EFVTFLFSKENSVWN HHHHHHHCCCCCCHH	41.00	24719451
379	Phosphorylation	PDGMPVIYHGHTLTT CCCCEEEEECCEEEE	11.28	-
389	Ubiquitination	HTLTTKIKFSDVLHT CEEEEEEEHHHHHHH	40.13	21890473
389	Ubiquitination	HTLTTKIKFSDVLHT CEEEEEEEHHHHHHH	40.13	21890473
412	Phosphorylation	SEYPVILSIEDHCSI CCCCEEEEEEHHCHH	16.89	-
428	Phosphorylation	QQRNMAQYFKKVLGD HHHHHHHHHHHHHCC	14.08	22461510
430	Ubiquitination	RNMAQYFKKVLGDTL HHHHHHHHHHHCCCC	36.72	-
430 (in isoform 2)	Ubiquitination	-	36.72	-
431	Ubiquitination	NMAQYFKKVLGDTLL HHHHHHHHHHCCCCC	32.56	21890473
431	Ubiquitination	NMAQYFKKVLGDTLL HHHHHHHHHHCCCCC	32.56	21890473
431 (in isoform 2)	Ubiquitination	-	32.56	-
440	Ubiquitination	LGDTLLTKPVEISAD HCCCCCCCCEEECCC	47.22	21890473
440 (in isoform 2)	Ubiquitination	-	47.22	-
451	Phosphorylation	ISADGLPSPNQLKRK ECCCCCCCHHHHHHH	41.34	25159151
456	Ubiquitination	LPSPNQLKRKILIKH CCCHHHHHHHHHHCH	41.71	-
456 (in isoform 2)	Ubiquitination	-	41.71	-
465	Ubiquitination	KILIKHKKLAEGSAY HHHHCHHHHCCCCCC	53.28	-
465 (in isoform 2)	Ubiquitination	-	53.28	-
470	Phosphorylation	HKKLAEGSAYEEVPT HHHHCCCCCCCCCCC	21.12	21945579
472	Phosphorylation	KLAEGSAYEEVPTSM HHCCCCCCCCCCCHH	17.83	21945579
477	Phosphorylation	SAYEEVPTSMMYSEN CCCCCCCCHHHCCCC	34.14	21945579
478	Phosphorylation	AYEEVPTSMMYSEND CCCCCCCHHHCCCCH	8.76	21945579
481	Phosphorylation	EVPTSMMYSENDISN CCCCHHHCCCCHHCH	12.28	21945579
482	Phosphorylation	VPTSMMYSENDISNS CCCHHHCCCCHHCHH	16.42	21945579
487	Phosphorylation	MYSENDISNSIKNGI HCCCCHHCHHHHCCE	27.64	21945579
489	Phosphorylation	SENDISNSIKNGILY CCCHHCHHHHCCEEE	28.31	21945579
496	Phosphorylation	SIKNGILYLEDPVNH HHHCCEEEEECCCCC	13.21	26356563
506	Phosphorylation	DPVNHEWYPHYFVLT CCCCCCCCCEEEEEE	4.16	26356563
509	Phosphorylation	NHEWYPHYFVLTSSK CCCCCCEEEEEECCE	7.29	26356563
513	Phosphorylation	YPHYFVLTSSKIYYS CCEEEEEECCEEEEE	26.17	26356563
514	Phosphorylation	PHYFVLTSSKIYYSE CEEEEEECCEEEEEC	26.02	26356563
515	Phosphorylation	HYFVLTSSKIYYSEE EEEEEECCEEEEECC	20.17	26356563
518	Phosphorylation	VLTSSKIYYSEETSS EEECCEEEEECCCCC	12.50	28450419
519	Phosphorylation	LTSSKIYYSEETSSD EECCEEEEECCCCCC	17.06	28450419
520	Phosphorylation	TSSKIYYSEETSSDQ ECCEEEEECCCCCCC	16.40	28450419
523	Phosphorylation	KIYYSEETSSDQGNE EEEEECCCCCCCCCC	29.49	25159151
524	Phosphorylation	IYYSEETSSDQGNED EEEECCCCCCCCCCC	34.89	25159151
525	Phosphorylation	YYSEETSSDQGNEDE EEECCCCCCCCCCCC	41.18	23927012
539	Phosphorylation	EEEPKEVSSSTELHS CCCCCCCCCCCCCCC	21.47	25159151
540	Phosphorylation	EEPKEVSSSTELHSN CCCCCCCCCCCCCCC	46.59	23186163
541	Phosphorylation	EPKEVSSSTELHSNE CCCCCCCCCCCCCCC	20.56	23186163
542	Phosphorylation	PKEVSSSTELHSNEK CCCCCCCCCCCCCCC	44.51	23927012
546	Phosphorylation	SSSTELHSNEKWFHG CCCCCCCCCCCCCCC	60.35	23186163
549	Ubiquitination	TELHSNEKWFHGKLG CCCCCCCCCCCCCCC	60.45	-
554	Ubiquitination	NEKWFHGKLGAGRDG CCCCCCCCCCCCCCH	34.87	-
554 (in isoform 2)	Ubiquitination	-	34.87	-
582	Phosphorylation	ETGAPDGSFLVRESE HHCCCCCCEEEEECC	23.84	28857561
666	Ubiquitination	QTNAHESKEWYHASL CCCCCCCHHHHHHHC	49.64	-
666 (in isoform 2)	Ubiquitination	-	49.64	-
669	Phosphorylation	AHESKEWYHASLTRA CCCCHHHHHHHCHHH	6.65	-
701	Phosphorylation	RKRNEPNSYAISFRA EECCCCCCEEEEEEE	27.02	28152594
702	Phosphorylation	KRNEPNSYAISFRAE ECCCCCCEEEEEEEE	18.00	28152594
705	Phosphorylation	EPNSYAISFRAEGKI CCCCEEEEEEEECCC	10.66	28152594
763	Ubiquitination	INEEALEKIGTAEPD CCHHHHHHHCCCCCC	47.49	-
763 (in isoform 2)	Ubiquitination	-	47.49	-
766	Phosphorylation	EALEKIGTAEPDYGA HHHHHHCCCCCCCCC	31.18	21945579
771	Phosphorylation	IGTAEPDYGALYEGR HCCCCCCCCCCCCCC	18.27	21945579
775	Phosphorylation	EPDYGALYEGRNPGF CCCCCCCCCCCCCCC	18.79	21945579
783	Phosphorylation	EGRNPGFYVEANPMP CCCCCCCEEECCCCC	11.86	25159151
791	Phosphorylation	VEANPMPTFKCAVKA EECCCCCCHHHHHHH	29.49	21945579
793	Ubiquitination	ANPMPTFKCAVKALF CCCCCCHHHHHHHHH	24.62	-
793 (in isoform 2)	Ubiquitination	-	24.62	-
797	Ubiquitination	PTFKCAVKALFDYKA CCHHHHHHHHHCHHC	22.35	-
797 (in isoform 2)	Ubiquitination	-	22.35	-
803	Ubiquitination	VKALFDYKAQREDEL HHHHHCHHCCCCCHH	39.63	-
815	Phosphorylation	DELTFIKSAIIQNVE CHHHHHHHHHHCCEE	21.64	27251275
823	Ubiquitination	AIIQNVEKQEGGWWR HHHCCEEECCCCCCC	49.74	-
833	Phosphorylation	GGWWRGDYGGKKQLW CCCCCCCCCCCEEEE	30.51	25839225
890	Ubiquitination	IAIRPEGKNNRLFVF EEECCCCCCCEEEEE	49.76	-
890 (in isoform 2)	Ubiquitination	-	49.76	-
932	Phosphorylation	KIREVAQTADARLTE HHHHHHHHHHHHCCC	19.43	28509920
941	Ubiquitination	DARLTEGKIMERRKK HHHCCCCHHHHHHHH	32.42	21890473
941	Acetylation	DARLTEGKIMERRKK HHHCCCCHHHHHHHH	32.42	25953088
941	Ubiquitination	DARLTEGKIMERRKK HHHCCCCHHHHHHHH	32.42	21890473
941 (in isoform 2)	Ubiquitination	-	32.42	-
954	Phosphorylation	KKIALELSELVVYCR HHHHHHHHHHEEEEE	21.36	-
959	Phosphorylation	ELSELVVYCRPVPFD HHHHHEEEEECCCCC	3.85	-
972	Phosphorylation	FDEEKIGTERACYRD CCHHHHCCCCHHCCC	26.27	24719451
977	Phosphorylation	IGTERACYRDMSSFP HCCCCHHCCCHHHCC	14.52	25159151
981	Phosphorylation	RACYRDMSSFPETKA CHHCCCHHHCCHHHH	32.87	30576142
982	Phosphorylation	ACYRDMSSFPETKAE HHCCCHHHCCHHHHH	37.88	30576142
987	Acetylation	MSSFPETKAEKYVNK HHHCCHHHHHHHHHH	53.54	25953088
987	Ubiquitination	MSSFPETKAEKYVNK HHHCCHHHHHHHHHH	53.54	-
987 (in isoform 2)	Ubiquitination	-	53.54	-
990	Acetylation	FPETKAEKYVNKAKG CCHHHHHHHHHHHHC	60.40	25953088
991	Phosphorylation	PETKAEKYVNKAKGK CHHHHHHHHHHHHCC	10.76	-
999	Acetylation	VNKAKGKKFLQYNRL HHHHHCCHHHHHCCE	61.03	25953088
1003	Phosphorylation	KGKKFLQYNRLQLSR HCCHHHHHCCEEHHC	12.37	29496907
1079	Ubiquitination	EAFDPFDKSSLRGLE CCCCCCCHHHCCCCC	42.18	-
1079 (in isoform 2)	Ubiquitination	-	42.18	-
1128	Phosphorylation	YDSTKQKTEFVVDNG CCCCCCEEEEEECCC	31.96	22468782
1150	Phosphorylation	KPFHFQISNPEFAFL CCEEEEECCCCEEEE	35.23	22468782
1162	Phosphorylation	AFLRFVVYEEDMFSD EEEEEEEEEHHHCCC	14.32	-
1193	Ubiquitination	GYRAVPLKNNYSEDL CEEEEECCCCCCCCH	36.76	-
1193 (in isoform 2)	Ubiquitination	-	36.76	-
1196	Phosphorylation	AVPLKNNYSEDLELA EEECCCCCCCCHHHH	23.88	29496907
1215 (in isoform 2)	Ubiquitination	-	52.53	-
1221	Phosphorylation	AKENGDLSPFSGTSL CCCCCCCCCCCCCCH	28.74	19664994
1222 (in isoform 2)	Phosphorylation	-	34.42	30266825
1224	Phosphorylation	NGDLSPFSGTSLRER CCCCCCCCCCCHHHC	44.54	30266825
1225 (in isoform 2)	Phosphorylation	-	21.50	27987026
1226	Phosphorylation	DLSPFSGTSLRERGS CCCCCCCCCHHHCCC	24.32	30266825
1227	Phosphorylation	LSPFSGTSLRERGSD CCCCCCCCHHHCCCC	29.02	30266825
1227 (in isoform 2)	Phosphorylation	-	29.02	27987026
1228 (in isoform 2)	Phosphorylation	-	7.09	22199227
1231	Methylation	SGTSLRERGSDASGQ CCCCHHHCCCCCCCC	43.40	115487745
1233	Phosphorylation	TSLRERGSDASGQLF CCHHHCCCCCCCCCC	35.90	25159151
1236	Phosphorylation	RERGSDASGQLFHGR HHCCCCCCCCCCCCC	31.87	23927012
1243	Methylation	SGQLFHGRAREGSFE CCCCCCCCCCCCCCH	23.15	115487755
1248	Phosphorylation	HGRAREGSFESRYQQ CCCCCCCCCHHHCCC	22.53	23401153
1251	Phosphorylation	AREGSFESRYQQPFE CCCCCCHHHCCCCHH	33.99	29255136
1253	Phosphorylation	EGSFESRYQQPFEDF CCCCHHHCCCCHHHC	22.30	23927012
1263	Phosphorylation	PFEDFRISQEHLADH CHHHCCCCHHHHHHH	25.84	23401153
1273	Phosphorylation	HLADHFDSRERRAPR HHHHHCCCCCCCCCC	34.79	29255136
1283	Methylation	RRAPRRTRVNGDNRL CCCCCCCCCCCCCCC	20.35	115487765

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
771	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
771	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
771	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
771	Y	Phosphorylation	Kinase	LCK	P06239	GPS
771	Y	Phosphorylation	Kinase	SYK	P43405	Uniprot
783	Y	Phosphorylation	Kinase	SYK	P43405	Uniprot
783	Y	Phosphorylation	Kinase	TXK	P42681	Uniprot
783	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
783	Y	Phosphorylation	Kinase	RET	P07949	PSP
783	Y	Phosphorylation	Kinase	PDGFRB	P09619	PSP
783	Y	Phosphorylation	Kinase	LCK	P06239	GPS
783	Y	Phosphorylation	Kinase	ITK	Q08881	Uniprot
783	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
1003	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
1248	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1248	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
1248	S	Phosphorylation	Kinase	AKT1	P31749	PSP
1248	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
1248	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
1253	Y	Phosphorylation	Kinase	EGFR	P00533	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	CBLB	Q13191	PMID:15308098
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:16467851
-	K	Ubiquitination	E3 ubiquitin ligase	ITCH	Q96J02	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:18671761

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PLCG1_HUMAN !!

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 PLCG1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EF1A1_HUMAN	EEF1A1	physical	11886851
GIT1_HUMAN	GIT1	physical	14523024
LYAM2_HUMAN	SELE	physical	12960351
PLD2_HUMAN	PLD2	physical	12646582
SRC_HUMAN	SRC	physical	7510703
WASP_HUMAN	WAS	physical	8805332
VAV_HUMAN	VAV1	physical	9891995
KHDR1_HUMAN	KHDRBS1	physical	11960376
GAB1_HUMAN	GAB1	physical	11507676
LCP2_HUMAN	LCP2	physical	11390650
GRB2_HUMAN	GRB2	physical	9281317
KHDR1_HUMAN	KHDRBS1	physical	9743338
RASA1_HUMAN	RASA1	physical	9743338
3BP2_HUMAN	SH3BP2	physical	11390470
KSYK_HUMAN	SYK	physical	7831290
LAT_HUMAN	LAT	physical	9729044
RHOA_HUMAN	RHOA	physical	12071848
PKN2_HUMAN	PKN2	physical	8910519
ALK_HUMAN	ALK	physical	11888936
PAK1_HUMAN	PAK1	physical	12085993
FAK1_HUMAN	PTK2	physical	10430888
KPCD1_HUMAN	PRKD1	physical	8885868
HNRPQ_HUMAN	SYNCRIP	physical	9341187
PGFRA_HUMAN	PDGFRA	physical	7535778
NTRK1_HUMAN	NTRK1	physical	10092678
NTRK2_HUMAN	NTRK2	physical	10092678
NTRK3_HUMAN	NTRK3	physical	10092678
RET_HUMAN	RET	physical	8628282
TNK1_HUMAN	TNK1	physical	10873601
KIT_HUMAN	KIT	physical	7536744
ERBB2_HUMAN	ERBB2	physical	1676673
ERBB2_HUMAN	ERBB2	physical	1683701
WASP_HUMAN	WAS	physical	8824280
CBL_HUMAN	CBL	physical	12061819
CBL_HUMAN	CBL	physical	9712732
IRS2_HUMAN	IRS2	physical	9535722
SOS1_HUMAN	SOS1	physical	10913276
GHR_HUMAN	GHR	physical	9632636
SOS2_HUMAN	SOS2	physical	10940929
TUB_HUMAN	TUB	physical	10455176
EGFR_HUMAN	EGFR	physical	9207933
GAB2_HUMAN	GAB2	physical	10391903
GELS_HUMAN	GSN	physical	9164868
PLXB1_HUMAN	PLXNB1	physical	19805522
PLXB2_HUMAN	PLXNB2	physical	19805522
CBL_HUMAN	CBL	physical	12941616
BLNK_HUMAN	BLNK	physical	10684856
CBL_HUMAN	CBL	physical	12803489
EGFR_HUMAN	EGFR	physical	12803489
EF1A1_HUMAN	EEF1A1	physical	12898421
IBTK_HUMAN	IBTK	physical	18596081
SPY1_HUMAN	SPRY1	physical	19915061
CBL_HUMAN	CBL	physical	16467851
VAV_HUMAN	VAV1	physical	16467851
LCP2_HUMAN	LCP2	physical	16467851
ZAP70_HUMAN	ZAP70	physical	16467851
LAT_HUMAN	LAT	physical	16467851
ERBB3_HUMAN	ERBB3	physical	16273093
KHDR1_HUMAN	KHDRBS1	physical	8977179
RASA1_HUMAN	RASA1	physical	8977179
EHD4_HUMAN	EHD4	physical	22863883
TF3C4_HUMAN	GTF3C4	physical	22863883
LIMD1_HUMAN	LIMD1	physical	22863883
PYGB_HUMAN	PYGB	physical	22863883
AKT1_HUMAN	AKT1	physical	16525023
PYRG1_HUMAN	CTPS1	physical	26344197
MCMBP_HUMAN	MCMBP	physical	26344197
PEPL1_HUMAN	NPEPL1	physical	26344197
SKIV2_HUMAN	SKIV2L	physical	26344197
TIPRL_HUMAN	TIPRL	physical	26344197
UN45A_HUMAN	UNC45A	physical	26344197
EGFR_HUMAN	EGFR	physical	11983899
PTN6_HUMAN	PTPN6	physical	27221712
EGFR_HUMAN	EGFR	physical	19605547
FGFR2_HUMAN	FGFR2	physical	15629145
GRB2_HUMAN	GRB2	physical	16038803

Drug and Disease Associations

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

Regulatory Network of PLCG1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6 AND SER-525, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771; TYR-775; TYR-783;SER-1221; TYR-1253 AND SER-1263, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6 AND SER-525, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1221, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1263, AND MASSSPECTROMETRY.	18220336 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771; TYR-775 ANDTYR-783, AND MASS SPECTROMETRY.	19534553 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771; TYR-783 ANDTYR-1253, AND MASS SPECTROMETRY.	17389395 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-977, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-1253, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-775, ANDMASS SPECTROMETRY.	15592455 [Abstract]
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules."; Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.; Mol. Cell. Proteomics 4:1240-1250(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-775 AND TYR-783, ANDMASS SPECTROMETRY.	15951569 [Abstract]
"Vascular endothelial growth factor (VEGF)-D and VEGF-A differentiallyregulate KDR-mediated signaling and biological function in vascularendothelial cells."; Jia H., Bagherzadeh A., Bicknell R., Duchen M.R., Liu D., Zachary I.; J. Biol. Chem. 279:36148-36157(2004). Cited for: PHOSPHORYLATION AT TYR-783 IN RESPONSE TO KDR ACTIVATION.	15215251 [Abstract]
"Membrane raft-dependent regulation of phospholipase Cgamma-1activation in T lymphocytes."; Veri M.C., DeBell K.E., Seminario M.C., DiBaldassarre A., Reischl I.,Rawat R., Graham L., Noviello C., Rellahan B.L., Miscia S.,Wange R.L., Bonvini E.; Mol. Cell. Biol. 21:6939-6950(2001). Cited for: PHOSPHORYLATION AT TYR-783, AND SUBCELLULAR LOCATION.	11564877 [Abstract]
"Phospholipase C-gamma1 interacts with conserved phosphotyrosylresidues in the linker region of Syk and is a substrate for Syk."; Law C.L., Chandran K.A., Sidorenko S.P., Clark E.A.; Mol. Cell. Biol. 16:1305-1315(1996). Cited for: PHOSPHORYLATION AT TYR-771 AND TYR-783 BY SYK, AND INTERACTION WITHSYK.	8657103 [Abstract]