dbPTM

TALDO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TALDO_HUMAN
UniProt AC	P37837
Protein Name	Transaldolase
Gene Name	TALDO1
Organism	Homo sapiens (Human).
Sequence Length	337
Subcellular Localization	Cytoplasm .
Protein Description	Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway..
Protein Sequence	MSSSPVKRQRMESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQHGIHCNMTLLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDFLTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTERMFNAENGK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSSPVKRQ ------CCCCHHHHH	39.25	23401153
3	Phosphorylation	-----MSSSPVKRQR -----CCCCHHHHHH	37.04	23401153
4	Phosphorylation	----MSSSPVKRQRM ----CCCCHHHHHHH	26.80	29255136
7	Acetylation	-MSSSPVKRQRMESA -CCCCHHHHHHHHHH	46.31	25953088
11	Sulfoxidation	SPVKRQRMESALDQL CHHHHHHHHHHHHHH	3.45	21406390
13	Phosphorylation	VKRQRMESALDQLKQ HHHHHHHHHHHHHHH	25.45	26074081
68	Phosphorylation	LVEEAIAYGRKLGGS HHHHHHHHHHHCCCC	16.02	30576742
71	Ubiquitination	EAIAYGRKLGGSQED HHHHHHHHCCCCHHH	47.31	21906983
75	Phosphorylation	YGRKLGGSQEDQIKN HHHHCCCCHHHHHHH	28.70	25159151
81	Ubiquitination	GSQEDQIKNAIDKLF CCHHHHHHHHHHHHH	34.39	21906983
105	Phosphorylation	KIPGRVSTEVDARLS HCCCCCCCCHHHHHC	36.85	-
115	Ubiquitination	DARLSFDKDAMVARA HHHHCCCHHHHHHHH	45.43	21906983
115	Acetylation	DARLSFDKDAMVARA HHHHCCCHHHHHHHH	45.43	26822725
115	2-Hydroxyisobutyrylation	DARLSFDKDAMVARA HHHHCCCHHHHHHHH	45.43	-
115	Ubiquitination	DARLSFDKDAMVARA HHHHCCCHHHHHHHH	45.43	21890473
118	Sulfoxidation	LSFDKDAMVARARRL HCCCHHHHHHHHHHH	3.29	21406390
130	Ubiquitination	RRLIELYKEAGISKD HHHHHHHHHHCCCCC	54.43	21890473
130	Malonylation	RRLIELYKEAGISKD HHHHHHHHHHCCCCC	54.43	26320211
130	2-Hydroxyisobutyrylation	RRLIELYKEAGISKD HHHHHHHHHHCCCCC	54.43	-
130	Ubiquitination	RRLIELYKEAGISKD HHHHHHHHHHCCCCC	54.43	21890473
130	Acetylation	RRLIELYKEAGISKD HHHHHHHHHHCCCCC	54.43	25953088
136	Acetylation	YKEAGISKDRILIKL HHHHCCCCCCEEEEE	49.45	23749302
136	Ubiquitination	YKEAGISKDRILIKL HHHHCCCCCCEEEEE	49.45	-
142	Ubiquitination	SKDRILIKLSSTWEG CCCCEEEEECCCCCH	38.58	-
145	Phosphorylation	RILIKLSSTWEGIQA CEEEEECCCCCHHHH	48.23	23403867
146	Phosphorylation	ILIKLSSTWEGIQAG EEEEECCCCCHHHHH	24.94	23403867
203	2-Hydroxyisobutyrylation	WHVANTDKKSYEPLE HHHCCCCCCCCCCCC	41.39	-
203	Ubiquitination	WHVANTDKKSYEPLE HHHCCCCCCCCCCCC	41.39	-
203	Acetylation	WHVANTDKKSYEPLE HHHCCCCCCCCCCCC	41.39	23749302
204	Ubiquitination	HVANTDKKSYEPLED HHCCCCCCCCCCCCC	62.17	21906983
204	2-Hydroxyisobutyrylation	HVANTDKKSYEPLED HHCCCCCCCCCCCCC	62.17	-
205	Phosphorylation	VANTDKKSYEPLEDP HCCCCCCCCCCCCCC	40.23	28152594
206	Phosphorylation	ANTDKKSYEPLEDPG CCCCCCCCCCCCCCC	30.37	28152594
206	Nitration	ANTDKKSYEPLEDPG CCCCCCCCCCCCCCC	30.37	-
215	2-Hydroxyisobutyrylation	PLEDPGVKSVTKIYN CCCCCCCCHHHHHHH	45.16	-
215	Ubiquitination	PLEDPGVKSVTKIYN CCCCCCCCHHHHHHH	45.16	21906983
215	Ubiquitination	PLEDPGVKSVTKIYN CCCCCCCCHHHHHHH	45.16	21890473
215	Acetylation	PLEDPGVKSVTKIYN CCCCCCCCHHHHHHH	45.16	27452117
219	Acetylation	PGVKSVTKIYNYYKK CCCCHHHHHHHHHHH	40.83	19608861
219	Ubiquitination	PGVKSVTKIYNYYKK CCCCHHHHHHHHHHH	40.83	21890473
219	Ubiquitination	PGVKSVTKIYNYYKK CCCCHHHHHHHHHHH	40.83	21906983
225	Succinylation	TKIYNYYKKFSYKTI HHHHHHHHHCCCEEE	36.66	23954790
225	2-Hydroxyisobutyrylation	TKIYNYYKKFSYKTI HHHHHHHHHCCCEEE	36.66	-
225	Acetylation	TKIYNYYKKFSYKTI HHHHHHHHHCCCEEE	36.66	26051181
228	Phosphorylation	YNYYKKFSYKTIVMG HHHHHHCCCEEEEEC	34.30	29496963
229	Phosphorylation	NYYKKFSYKTIVMGA HHHHHCCCEEEEECC	18.45	20068231
230	Ubiquitination	YYKKFSYKTIVMGAS HHHHCCCEEEEECCC	30.49	21890473
230	Ubiquitination	YYKKFSYKTIVMGAS HHHHCCCEEEEECCC	30.49	21906983
231	Phosphorylation	YKKFSYKTIVMGASF HHHCCCEEEEECCCC	15.57	23403867
234	Sulfoxidation	FSYKTIVMGASFRNT CCCEEEEECCCCCCC	3.07	21406390
237	Phosphorylation	KTIVMGASFRNTGEI EEEEECCCCCCCCCC	21.00	25159151
241	Phosphorylation	MGASFRNTGEIKALA ECCCCCCCCCCHHHC	31.75	20068231
245	Ubiquitination	FRNTGEIKALAGCDF CCCCCCCHHHCCCCE	32.80	-
245	2-Hydroxyisobutyrylation	FRNTGEIKALAGCDF CCCCCCCHHHCCCCE	32.80	-
250	S-nitrosylation	EIKALAGCDFLTISP CCHHHCCCCEEEECH	2.52	25040305
250	Glutathionylation	EIKALAGCDFLTISP CCHHHCCCCEEEECH	2.52	22555962
254	Phosphorylation	LAGCDFLTISPKLLG HCCCCEEEECHHHHH	21.28	29255136
256	Phosphorylation	GCDFLTISPKLLGEL CCCEEEECHHHHHHH	15.67	29255136
258	Ubiquitination	DFLTISPKLLGELLQ CEEEECHHHHHHHHH	49.94	21906983
269	Ubiquitination	ELLQDNAKLVPVLSA HHHHHCCCCHHHHCH	57.16	21906983
269	Ubiquitination	ELLQDNAKLVPVLSA HHHHHCCCCHHHHCH	57.16	21890473
269	2-Hydroxyisobutyrylation	ELLQDNAKLVPVLSA HHHHHCCCCHHHHCH	57.16	-
269	Acetylation	ELLQDNAKLVPVLSA HHHHHCCCCHHHHCH	57.16	19608861
275	Phosphorylation	AKLVPVLSAKAAQAS CCCHHHHCHHHHCCC	28.14	21712546
277	Ubiquitination	LVPVLSAKAAQASDL CHHHHCHHHHCCCCH	40.66	21890473
277	2-Hydroxyisobutyrylation	LVPVLSAKAAQASDL CHHHHCHHHHCCCCH	40.66	-
277	Acetylation	LVPVLSAKAAQASDL CHHHHCHHHHCCCCH	40.66	25953088
277	Malonylation	LVPVLSAKAAQASDL CHHHHCHHHHCCCCH	40.66	26320211
277	Ubiquitination	LVPVLSAKAAQASDL CHHHHCHHHHCCCCH	40.66	21890473
286	Acetylation	AQASDLEKIHLDEKS HCCCCHHHCCCCHHH	42.60	19608861
286	Malonylation	AQASDLEKIHLDEKS HCCCCHHHCCCCHHH	42.60	26320211
286	2-Hydroxyisobutyrylation	AQASDLEKIHLDEKS HCCCCHHHCCCCHHH	42.60	-
286	Ubiquitination	AQASDLEKIHLDEKS HCCCCHHHCCCCHHH	42.60	19608861
292	2-Hydroxyisobutyrylation	EKIHLDEKSFRWLHN HHCCCCHHHHHHHCC	55.34	-
292	Ubiquitination	EKIHLDEKSFRWLHN HHCCCCHHHHHHHCC	55.34	-
292	Acetylation	EKIHLDEKSFRWLHN HHCCCCHHHHHHHCC	55.34	26822725
303	Sulfoxidation	WLHNEDQMAVEKLSD HHCCHHHHHHHHHHH	7.54	30846556
307	Ubiquitination	EDQMAVEKLSDGIRK HHHHHHHHHHHHHHH	46.85	21906983
307	Ubiquitination	EDQMAVEKLSDGIRK HHHHHHHHHHHHHHH	46.85	21890473
307	Acetylation	EDQMAVEKLSDGIRK HHHHHHHHHHHHHHH	46.85	23236377
307	2-Hydroxyisobutyrylation	EDQMAVEKLSDGIRK HHHHHHHHHHHHHHH	46.85	-
314	Ubiquitination	KLSDGIRKFAADAVK HHHHHHHHHHHHHHH	37.12	21890473
314	Ubiquitination	KLSDGIRKFAADAVK HHHHHHHHHHHHHHH	37.12	21890473
314	Malonylation	KLSDGIRKFAADAVK HHHHHHHHHHHHHHH	37.12	26320211
314	Acetylation	KLSDGIRKFAADAVK HHHHHHHHHHHHHHH	37.12	25953088
321	Ubiquitination	KFAADAVKLERMLTE HHHHHHHHHHHHHHH	46.48	21890473
321	Acetylation	KFAADAVKLERMLTE HHHHHHHHHHHHHHH	46.48	19608861
321	2-Hydroxyisobutyrylation	KFAADAVKLERMLTE HHHHHHHHHHHHHHH	46.48	-
321	Malonylation	KFAADAVKLERMLTE HHHHHHHHHHHHHHH	46.48	26320211
321	Ubiquitination	KFAADAVKLERMLTE HHHHHHHHHHHHHHH	46.48	19608861
327	Phosphorylation	VKLERMLTERMFNAE HHHHHHHHHHHHCCC	16.53	-
337	Acetylation	MFNAENGK------- HHCCCCCC-------	69.61	61249
337	Ubiquitination	MFNAENGK------- HHCCCCCC-------	69.61	-

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
Oops, there are no upstream regulatory protein records of TALDO_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TKT_HUMAN	TKT	physical	22939629
CH10_HUMAN	HSPE1	physical	22863883
WDR1_HUMAN	WDR1	physical	22863883
SPC24_HUMAN	SPC24	physical	26186194
CFDP1_HUMAN	CFDP1	physical	26186194
ATG2B_HUMAN	ATG2B	physical	26186194
BRE1B_HUMAN	RNF40	physical	26186194
PDE6D_HUMAN	PDE6D	physical	26186194
PJA1_HUMAN	PJA1	physical	26186194
P73_HUMAN	TP73	physical	26186194
KAPCB_HUMAN	PRKACB	physical	26186194
WIPI4_HUMAN	WDR45	physical	26186194
PMF1_HUMAN	PMF1	physical	26186194
DENR_HUMAN	DENR	physical	26186194
ZN655_HUMAN	ZNF655	physical	26186194
AK1A1_HUMAN	AKR1A1	physical	26344197
PIPNB_HUMAN	PITPNB	physical	26344197
PSMG4_HUMAN	PSMG4	physical	26344197
SCYL2_HUMAN	SCYL2	physical	26344197
WIPI4_HUMAN	WDR45	physical	28514442
CFDP1_HUMAN	CFDP1	physical	28514442
PDE6D_HUMAN	PDE6D	physical	28514442
PMF1_HUMAN	PMF1	physical	28514442
SPC24_HUMAN	SPC24	physical	28514442
MRC2_HUMAN	MRC2	physical	28514442
ATG2B_HUMAN	ATG2B	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606003	Transaldolase deficiency (TALDOD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TALDO_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-219; LYS-269; LYS-286 ANDLYS-321, AND MASS SPECTROMETRY.	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-237, AND MASSSPECTROMETRY.	19690332 [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 SER-4, AND MASSSPECTROMETRY.	17081983 [Abstract]