TIGAR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TIGAR_HUMAN
• UniProt AC: Q9NQ88
• Protein Name: Fructose-2,6-bisphosphatase TIGAR {ECO:0000305}
• Gene Name: TIGAR {ECO:0000303|PubMed:16839880}
• Organism: Homo sapiens (Human).
• Sequence Length: 270
• Subcellular Localization: Cytoplasm . Nucleus . Mitochondrion . Translocated to the mitochondria during hypoxia in a HIF1A-dependent manner (PubMed:23185017). Colocalizes with HK2 in the mitochondria during hypoxia (PubMed:23185017). Translocated to the nucleus during hypoxia
• Protein Description: Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate. [PubMed: 19015259 Acts as a negative regulator of glycolysis by lowering intracellular levels of fructose-2,6-bisphosphate in a p53/TP53-dependent manner, resulting in the pentose phosphate pathway (PPP) activation and NADPH production]
• Protein Sequence: MARFALTVVRHGETRFNKEKIIQGQGVDEPLSETGFKQAAAAGIFLNNVKFTHAFSSDLMRTKQTMHGILERSKFCKDMTVKYDSRLRERKYGVVEGKALSELRAMAKAAREECPVFTPPGGETLDQVKMRGIDFFEFLCQLILKEADQKEQFSQGSPSNCLETSLAEIFPLGKNHSSKVNSDSGIPGLAASVLVVSHGAYMRSLFDYFLTDLKCSLPATLSRSELMSVTPNTGMSLFIINFEEGREVKPTVQCICMNLQDHLNGLTETR

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Ubiquitination	HGETRFNKEKIIQGQ CCCCCCCHHHHHCCC	58.64	22817900
20	Acetylation	ETRFNKEKIIQGQGV CCCCCHHHHHCCCCC	46.87	23236377
20	Malonylation	ETRFNKEKIIQGQGV CCCCCHHHHHCCCCC	46.87	26320211
20	Ubiquitination	ETRFNKEKIIQGQGV CCCCCHHHHHCCCCC	46.87	21906983
34	Phosphorylation	VDEPLSETGFKQAAA CCCCCCHHCHHHHHH	44.54	22817900
37	Ubiquitination	PLSETGFKQAAAAGI CCCHHCHHHHHHHCH	40.13	21906983
37	Methylation	PLSETGFKQAAAAGI CCCHHCHHHHHHHCH	40.13	42373057
50	Acetylation	GIFLNNVKFTHAFSS CHHHCCCCCCCCCCH	46.82	19608861
61	Methylation	AFSSDLMRTKQTMHG CCCHHHHHCHHHHHH	46.17	115918477
63	Ubiquitination	SSDLMRTKQTMHGIL CHHHHHCHHHHHHHH	33.15	29967540
80	Phosphorylation	SKFCKDMTVKYDSRL HHHHCCCCCEECHHH	24.79	-
82	Acetylation	FCKDMTVKYDSRLRE HHCCCCCEECHHHHH	33.89	26051181
83	Phosphorylation	CKDMTVKYDSRLRER HCCCCCEECHHHHHH	18.15	-
85	Phosphorylation	DMTVKYDSRLRERKY CCCCEECHHHHHHHC	30.08	-
91	Ubiquitination	DSRLRERKYGVVEGK CHHHHHHHCCEECCH	41.42	29967540
92	Phosphorylation	SRLRERKYGVVEGKA HHHHHHHCCEECCHH	22.75	29496907
98	Ubiquitination	KYGVVEGKALSELRA HCCEECCHHHHHHHH	32.42	24816145
101	Phosphorylation	VVEGKALSELRAMAK EECCHHHHHHHHHHH	39.17	-
129	2-Hydroxyisobutyrylation	GETLDQVKMRGIDFF CCCHHHHHHCCCCHH	19.76	-
129	Ubiquitination	GETLDQVKMRGIDFF CCCHHHHHHCCCCHH	19.76	24816145
150	Ubiquitination	ILKEADQKEQFSQGS HHHHHHHHHHHHCCC	54.77	29967540
154	Phosphorylation	ADQKEQFSQGSPSNC HHHHHHHHCCCCCHH	33.07	17525332
157	Phosphorylation	KEQFSQGSPSNCLET HHHHHCCCCCHHHHH	19.95	21712546
159	Phosphorylation	QFSQGSPSNCLETSL HHHCCCCCHHHHHHH	41.70	28464451
164	Phosphorylation	SPSNCLETSLAEIFP CCCHHHHHHHHHHCC	18.98	22199227
165	Phosphorylation	PSNCLETSLAEIFPL CCHHHHHHHHHHCCC	19.06	22199227
174	Ubiquitination	AEIFPLGKNHSSKVN HHHCCCCCCCCCCCC	60.20	29967540
182	Phosphorylation	NHSSKVNSDSGIPGL CCCCCCCCCCCCCCH	35.82	20068231
184	Phosphorylation	SSKVNSDSGIPGLAA CCCCCCCCCCCCHHH	38.14	20068231
192	Phosphorylation	GIPGLAASVLVVSHG CCCCHHHHHEHHCCC	15.46	20068231
197	Phosphorylation	AASVLVVSHGAYMRS HHHHEHHCCCHHHHH	14.55	20068231
201	Phosphorylation	LVVSHGAYMRSLFDY EHHCCCHHHHHHHHH	9.54	20068231
204	Phosphorylation	SHGAYMRSLFDYFLT CCCHHHHHHHHHHHH	19.50	21712546

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TIGAR_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TIGAR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
UB2L3_HUMAN	UBE2L3	physical	22939629
TSC2_HUMAN	TSC2	physical	22939629
RL11_HUMAN	RPL11	physical	21988832
PCBP1_HUMAN	PCBP1	physical	26344197
TKT_HUMAN	TKT	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-50, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
PubMed: 17525332

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND MASSSPECTROMETRY.
PubMed: 18187866