dbPTM

TAGL2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TAGL2_HUMAN
UniProt AC	P37802
Protein Name	Transgelin-2
Gene Name	TAGLN2
Organism	Homo sapiens (Human).
Sequence Length	199
Subcellular Localization
Protein Description
Protein Sequence	MANRGPAYGLSREVQQKIEKQYDADLEQILIQWITTQCRKDVGRPQPGRENFQNWLKDGTVLCELINALYPEGQAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFSGDPNWFPKKSKENPRNFSDNQLQEGKNVIGLQMGTNRGASQAGMTGYGMPRQIL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MANRGPAYG ------CCCCCCCCC	17.90	19413330
4	Methylation	----MANRGPAYGLS ----CCCCCCCCCCC	42.82	115367851
8	Phosphorylation	MANRGPAYGLSREVQ CCCCCCCCCCCHHHH	23.02	21945579
11	Phosphorylation	RGPAYGLSREVQQKI CCCCCCCCHHHHHHH	23.25	21945579
17	Acetylation	LSREVQQKIEKQYDA CCHHHHHHHHHHHCC	35.42	19608861
17	Ubiquitination	LSREVQQKIEKQYDA CCHHHHHHHHHHHCC	35.42	19608861
20	Acetylation	EVQQKIEKQYDADLE HHHHHHHHHHCCCHH	58.60	19608861
20	Ubiquitination	EVQQKIEKQYDADLE HHHHHHHHHHCCCHH	58.60	19608861
22	Phosphorylation	QQKIEKQYDADLEQI HHHHHHHHCCCHHHH	24.94	26846344
32	Phosphorylation	DLEQILIQWITTQCR CHHHHHHHHHHHHHH	23.29	27251275
35	Phosphorylation	QILIQWITTQCRKDV HHHHHHHHHHHHHCC	14.09	26846344
36	Phosphorylation	ILIQWITTQCRKDVG HHHHHHHHHHHHCCC	19.28	26846344
38	Acetylation	IQWITTQCRKDVGRP HHHHHHHHHHCCCCC	5.69	19608861
40	Ubiquitination	WITTQCRKDVGRPQP HHHHHHHHCCCCCCC	65.48	-
41	Acetylation	ITTQCRKDVGRPQPG HHHHHHHCCCCCCCC	28.84	19608861
57	Sumoylation	ENFQNWLKDGTVLCE HHHHHHHHHCHHHHH	45.81	-
60	Phosphorylation	QNWLKDGTVLCELIN HHHHHHCHHHHHHHH	22.04	21712546
63	Glutathionylation	LKDGTVLCELINALY HHHCHHHHHHHHHHC	3.30	22555962
78	Ubiquitination	PEGQAPVKKIQASTM CCCCCCHHHHHHHHH	43.00	-
78	Succinylation	PEGQAPVKKIQASTM CCCCCCHHHHHHHHH	43.00	23954790
78	Acetylation	PEGQAPVKKIQASTM CCCCCCHHHHHHHHH	43.00	7462009
79	Sumoylation	EGQAPVKKIQASTMA CCCCCHHHHHHHHHH	40.04	-
79	Malonylation	EGQAPVKKIQASTMA CCCCCHHHHHHHHHH	40.04	26320211
79	Sumoylation	EGQAPVKKIQASTMA CCCCCHHHHHHHHHH	40.04	-
79	Ubiquitination	EGQAPVKKIQASTMA CCCCCHHHHHHHHHH	40.04	-
83	Phosphorylation	PVKKIQASTMAFKQM CHHHHHHHHHHHHHH	11.44	21577206
83	O-linked_Glycosylation	PVKKIQASTMAFKQM CHHHHHHHHHHHHHH	11.44	23301498
84	Phosphorylation	VKKIQASTMAFKQME HHHHHHHHHHHHHHH	18.61	-
85	Sulfoxidation	KKIQASTMAFKQMEQ HHHHHHHHHHHHHHH	3.70	21406390
88	Acetylation	QASTMAFKQMEQISQ HHHHHHHHHHHHHHH	38.92	23236377
88	Ubiquitination	QASTMAFKQMEQISQ HHHHHHHHHHHHHHH	38.92	21906983
90	Sulfoxidation	STMAFKQMEQISQFL HHHHHHHHHHHHHHH	4.16	28465586
94	Phosphorylation	FKQMEQISQFLQAAE HHHHHHHHHHHHHHH	17.99	21712546
120	Ubiquitination	TVDLWEGKNMACVQR HCCCCCCCCHHHHHH	31.84	-
120	Acetylation	TVDLWEGKNMACVQR HCCCCCCCCHHHHHH	31.84	23236377
128	Phosphorylation	NMACVQRTLMNLGGL CHHHHHHHHHHHCCE	17.17	23911959
130	Sulfoxidation	ACVQRTLMNLGGLAV HHHHHHHHHHCCEEE	3.73	21406390
139	Methylation	LGGLAVARDDGLFSG HCCEEEECCCCCCCC	35.63	30763287
139	Dimethylation	LGGLAVARDDGLFSG HCCEEEECCCCCCCC	35.63	-
145	Phosphorylation	ARDDGLFSGDPNWFP ECCCCCCCCCCCCCC	47.53	21712546
153	Succinylation	GDPNWFPKKSKENPR CCCCCCCCCCCCCCC	61.27	23954790
153	Acetylation	GDPNWFPKKSKENPR CCCCCCCCCCCCCCC	61.27	23954790
153	Ubiquitination	GDPNWFPKKSKENPR CCCCCCCCCCCCCCC	61.27	-
154	Ubiquitination	DPNWFPKKSKENPRN CCCCCCCCCCCCCCC	67.98	-
155	Phosphorylation	PNWFPKKSKENPRNF CCCCCCCCCCCCCCC	51.86	26074081
156	Ubiquitination	NWFPKKSKENPRNFS CCCCCCCCCCCCCCC	71.09	-
163	Phosphorylation	KENPRNFSDNQLQEG CCCCCCCCHHHCCCC	38.92	29255136
163	O-linked_Glycosylation	KENPRNFSDNQLQEG CCCCCCCCHHHCCCC	38.92	23301498
166	Phosphorylation	PRNFSDNQLQEGKNV CCCCCHHHCCCCCCE	49.89	27251275
171	Sumoylation	DNQLQEGKNVIGLQM HHHCCCCCCEEEEEC	47.49	-
171	Ubiquitination	DNQLQEGKNVIGLQM HHHCCCCCCEEEEEC	47.49	21890473
171	Acetylation	DNQLQEGKNVIGLQM HHHCCCCCCEEEEEC	47.49	23954790
171	Sumoylation	DNQLQEGKNVIGLQM HHHCCCCCCEEEEEC	47.49	28112733
178	Sulfoxidation	KNVIGLQMGTNRGAS CCEEEEECCCCCCCH	9.57	28465586
180	Phosphorylation	VIGLQMGTNRGASQA EEEEECCCCCCCHHC	19.19	22617229
182	Methylation	GLQMGTNRGASQAGM EEECCCCCCCHHCCC	41.72	24129315
184	Phosphorylation	QMGTNRGASQAGMTG ECCCCCCCHHCCCCC	8.67	27251275
185	O-linked_Glycosylation	MGTNRGASQAGMTGY CCCCCCCHHCCCCCC	24.32	23301498
185	Phosphorylation	MGTNRGASQAGMTGY CCCCCCCHHCCCCCC	24.32	25159151
189	Sulfoxidation	RGASQAGMTGYGMPR CCCHHCCCCCCCCCC	2.70	28465586
190	O-linked_Glycosylation	GASQAGMTGYGMPRQ CCHHCCCCCCCCCCC	26.74	23301498
190	Phosphorylation	GASQAGMTGYGMPRQ CCHHCCCCCCCCCCC	26.74	21945579
192	Phosphorylation	SQAGMTGYGMPRQIL HHCCCCCCCCCCCCC	10.90	21945579
192	Nitration	SQAGMTGYGMPRQIL HHCCCCCCCCCCCCC	10.90	-
194	Sulfoxidation	AGMTGYGMPRQIL-- CCCCCCCCCCCCC--	1.54	28465586
196	Methylation	MTGYGMPRQIL---- CCCCCCCCCCC----	27.55	24129315
201	Phosphorylation	MPRQIL--------- CCCCCC---------		27251275
206	Phosphorylation	L-------------- C--------------		27251275

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
11	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
83	S	Phosphorylation	Kinase	CDK14	O94921	PSP
145	S	Phosphorylation	Kinase	ERK2	P28482	PSP
163	S	Phosphorylation	Kinase	CDK14	O94921	PSP
163	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
180	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
185	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TAGL2_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 TAGL2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
TOM40_HUMAN	TOMM40	physical	22939629
THIM_HUMAN	ACAA2	physical	26344197
ALDOA_HUMAN	ALDOA	physical	26344197
ALDOC_HUMAN	ALDOC	physical	26344197
ARL8A_HUMAN	ARL8A	physical	26344197
ATOX1_HUMAN	ATOX1	physical	26344197
NNRD_HUMAN	CARKD	physical	26344197
CLIC3_HUMAN	CLIC3	physical	26344197
CLIC4_HUMAN	CLIC4	physical	26344197
CRIP1_HUMAN	CRIP1	physical	26344197
DUT_HUMAN	DUT	physical	26344197
ECI1_HUMAN	ECI1	physical	26344197
EF2_HUMAN	EEF2	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
ENOG_HUMAN	ENO2	physical	26344197
ENOB_HUMAN	ENO3	physical	26344197
FABPH_HUMAN	FABP3	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
FABP7_HUMAN	FABP7	physical	26344197
FKB1A_HUMAN	FKBP1A	physical	26344197
FKB1B_HUMAN	FKBP1B	physical	26344197
GPX4_HUMAN	GPX4	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
C1TM_HUMAN	MTHFD1L	physical	26344197
NTF2_HUMAN	NUTF2	physical	26344197
PHB_HUMAN	PHB	physical	26344197
PIN1_HUMAN	PIN1	physical	26344197
PLST_HUMAN	PLS3	physical	26344197
MYP2_HUMAN	PMP2	physical	26344197
SERC_HUMAN	PSAT1	physical	26344197
RAB10_HUMAN	RAB10	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TKT_HUMAN	TKT	physical	26344197
TKTL2_HUMAN	TKTL2	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	28514442

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 TAGL2_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-163, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17 AND LYS-20, AND MASSSPECTROMETRY.	19608861 [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 SER-163 AND SER-185, ANDMASS 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-163, 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-163 AND SER-185, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-185, ANDMASS SPECTROMETRY.	18088087 [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-8 AND TYR-192, AND MASSSPECTROMETRY.	19534553 [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-192, AND MASSSPECTROMETRY.	18083107 [Abstract]