dbPTM

TAGL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TAGL_HUMAN
UniProt AC	Q01995
Protein Name	Transgelin
Gene Name	TAGLN
Organism	Homo sapiens (Human).
Sequence Length	201
Subcellular Localization	Cytoplasm .
Protein Description	Actin cross-linking/gelling protein (By similarity). Involved in calcium interactions and contractile properties of the cell that may contribute to replicative senescence..
Protein Sequence	MANKGPSYGMSREVQSKIEKKYDEELEERLVEWIIVQCGPDVGRPDRGRLGFQVWLKNGVILSKLVNSLYPDGSKPVKVPENPPSMVFKQMEQVAQFLKAAEDYGVIKTDMFQTVDLFEGKDMAAVQRTLMALGSLAVTKNDGHYRGDPNWFMKKAQEHKREFTESQLQEGKHVIGLQMGSNRGASQAGMTGYGRPRQIIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MANKGPSYG ------CCCCCCCCC	26.83	22814378
4	Acetylation	----MANKGPSYGMS ----CCCCCCCCCCC	63.76	7665153
4	Malonylation	----MANKGPSYGMS ----CCCCCCCCCCC	63.76	26320211
7	Phosphorylation	-MANKGPSYGMSREV -CCCCCCCCCCCHHH	42.88	21406692
8	Phosphorylation	MANKGPSYGMSREVQ CCCCCCCCCCCHHHH	21.71	21406692
11	Phosphorylation	KGPSYGMSREVQSKI CCCCCCCCHHHHHHH	22.41	21406692
16	Phosphorylation	GMSREVQSKIEKKYD CCCHHHHHHHHHHCC	40.55	26699800
17	Acetylation	MSREVQSKIEKKYDE CCHHHHHHHHHHCCH	37.48	23236377
20	Malonylation	EVQSKIEKKYDEELE HHHHHHHHHCCHHHH	61.17	26320211
21	Acetylation	VQSKIEKKYDEELEE HHHHHHHHCCHHHHH	45.18	27178108
21	Malonylation	VQSKIEKKYDEELEE HHHHHHHHCCHHHHH	45.18	26320211
22	Phosphorylation	QSKIEKKYDEELEER HHHHHHHCCHHHHHH	39.39	21253578
38	S-palmitoylation	VEWIIVQCGPDVGRP HHHHHHHCCCCCCCC	6.22	29575903
38	S-nitrosylation	VEWIIVQCGPDVGRP HHHHHHHCCCCCCCC	6.22	25040305
63	Phosphorylation	LKNGVILSKLVNSLY EECCCHHHHHHHHHC	16.90	21406692
64	Ubiquitination	KNGVILSKLVNSLYP ECCCHHHHHHHHHCC	53.67	-
68	Phosphorylation	ILSKLVNSLYPDGSK HHHHHHHHHCCCCCC	23.08	-
70	Phosphorylation	SKLVNSLYPDGSKPV HHHHHHHCCCCCCCC	10.09	-
75	Malonylation	SLYPDGSKPVKVPEN HHCCCCCCCCCCCCC	60.40	26320211
78	Malonylation	PDGSKPVKVPENPPS CCCCCCCCCCCCCCC	61.68	26320211
85	Phosphorylation	KVPENPPSMVFKQME CCCCCCCCHHHHHHH	28.92	27499020
86	Sulfoxidation	VPENPPSMVFKQMEQ CCCCCCCHHHHHHHH	5.18	30846556
89	Malonylation	NPPSMVFKQMEQVAQ CCCCHHHHHHHHHHH	37.01	26320211
91	Sulfoxidation	PSMVFKQMEQVAQFL CCHHHHHHHHHHHHH	3.92	30846556
99	Ubiquitination	EQVAQFLKAAEDYGV HHHHHHHHHHHHHCC	47.00	-
104	Phosphorylation	FLKAAEDYGVIKTDM HHHHHHHHCCEECCC	12.56	21253578
109	Phosphorylation	EDYGVIKTDMFQTVD HHHCCEECCCCCEEC	22.90	21712546
111	Sulfoxidation	YGVIKTDMFQTVDLF HCCEECCCCCEECCC	3.03	30846556
114	Phosphorylation	IKTDMFQTVDLFEGK EECCCCCEECCCCCC	12.53	27499020
123	Sulfoxidation	DLFEGKDMAAVQRTL CCCCCCCHHHHHHHH	2.69	30846556
129	Phosphorylation	DMAAVQRTLMALGSL CHHHHHHHHHHHCCE	12.09	20068231
131	Sulfoxidation	AAVQRTLMALGSLAV HHHHHHHHHHCCEEE	2.60	30846556
135	Phosphorylation	RTLMALGSLAVTKND HHHHHHCCEEEECCC	17.63	20068231
139	Phosphorylation	ALGSLAVTKNDGHYR HHCCEEEECCCCCCC	20.65	20068231
145	Phosphorylation	VTKNDGHYRGDPNWF EECCCCCCCCCCCHH	23.09	-
153	Sulfoxidation	RGDPNWFMKKAQEHK CCCCCHHHHHHHHHH	3.08	30846556
154	Acetylation	GDPNWFMKKAQEHKR CCCCHHHHHHHHHHH	35.17	27178108
155	Acetylation	DPNWFMKKAQEHKRE CCCHHHHHHHHHHHH	43.44	30592817
160	Acetylation	MKKAQEHKREFTESQ HHHHHHHHHHCCHHH	53.52	30592823
164	Phosphorylation	QEHKREFTESQLQEG HHHHHHCCHHHHHCC	29.94	26657352
166	O-linked_Glycosylation	HKREFTESQLQEGKH HHHHCCHHHHHCCCE	32.88	31373491
166	Phosphorylation	HKREFTESQLQEGKH HHHHCCHHHHHCCCE	32.88	28355574
172	Malonylation	ESQLQEGKHVIGLQM HHHHHCCCEEEEEEC	33.67	26320211
172	Acetylation	ESQLQEGKHVIGLQM HHHHHCCCEEEEEEC	33.67	-
179	Sulfoxidation	KHVIGLQMGSNRGAS CEEEEEECCCCCCCH	8.37	30846556
181	Phosphorylation	VIGLQMGSNRGASQA EEEEECCCCCCCHHC	20.29	22617229
183	Methylation	GLQMGSNRGASQAGM EEECCCCCCCHHCCC	43.69	24129315
186	Phosphorylation	MGSNRGASQAGMTGY CCCCCCCHHCCCCCC	24.32	21712546
190	Sulfoxidation	RGASQAGMTGYGRPR CCCHHCCCCCCCCCC	2.70	30846556
191	Phosphorylation	GASQAGMTGYGRPRQ CCHHCCCCCCCCCCC	26.74	26356563
191	O-linked_Glycosylation	GASQAGMTGYGRPRQ CCHHCCCCCCCCCCC	26.74	31373491
193	Phosphorylation	SQAGMTGYGRPRQII HHCCCCCCCCCCCCC	10.78	21082442
195	Methylation	AGMTGYGRPRQIIS- CCCCCCCCCCCCCC-	18.10	18959177

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
181	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
181	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
181	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S10A9_HUMAN	S100A9	physical	17353931
ACTS_HUMAN	ACTA1	physical	11053353
PK3CD_HUMAN	PIK3CD	physical	22798525
JAK1_HUMAN	JAK1	physical	22798525
DUS6_HUMAN	DUSP6	physical	25515236
THIM_HUMAN	ACAA2	physical	26344197
ALDOA_HUMAN	ALDOA	physical	26344197
ALDOC_HUMAN	ALDOC	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
NTF2_HUMAN	NUTF2	physical	26344197
6PGD_HUMAN	PGD	physical	26344197
PLST_HUMAN	PLS3	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
UCHL3_HUMAN	UCHL3	physical	26344197

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 TAGL_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-193, AND MASSSPECTROMETRY.	18083107 [Abstract]