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Protein

Fructose-2,6-bisphosphatase TIGAR

Gene

TIGAR

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Fructose-bisphosphatase hydrolyzing fructose-2,6-bisphosphate as well as fructose-1,6-bisphosphate (By similarity). 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. Contributes to the generation of reduced glutathione to cause a decrease in intracellular reactive oxygen species (ROS) content, correlating with its ability to protect cells from oxidative or metabolic stress-induced cell death. Plays a role in promoting protection against cell death during hypoxia by decreasing mitochondria ROS levels in a HK2-dependent manner through a mechanism that is independent of its fructose-bisphosphatase activity. In response to cardiac damage stress, mediates p53-induced inhibition of myocyte mitophagy through ROS levels reduction and the subsequent inactivation of BNIP3. Reduced mitophagy results in an enhanced apoptotic myocyte cell death, and exacerbates cardiac damage. Plays a role in adult intestinal regeneration; contributes to the growth, proliferation and survival of intestinal crypts following tissue ablation. Plays a neuroprotective role against ischemic brain damage by enhancing PPP flux and preserving mitochondria functions. Protects glioma cells from hypoxia- and ROS-induced cell death by inhibiting glycolysis and activating mitochondrial energy metabolism and oxygen consumption in a TKTL1-dependent and p53/TP53-independent manner. Plays a role in cancer cell survival by promoting DNA repair through activating PPP flux in a CDK5-ATM-dependent signaling pathway during hypoxia and/or genome stress-induced DNA damage responses. Involved in intestinal tumor progression.By similarity

Caution

Not expected to have any kinase activity.Curated

Catalytic activityi

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei11Tele-phosphohistidine intermediateBy similarity1
Active sitei89Proton donor/acceptorBy similarity1
Sitei198Transition state stabilizerBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processApoptosis, Autophagy

Enzyme and pathway databases

ReactomeiR-BTA-5628897 TP53 Regulates Metabolic Genes

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-2,6-bisphosphatase TIGARCurated (EC:3.1.3.46By similarity)
Alternative name(s):
TP53-induced glycolysis and apoptosis regulatorBy similarity
TP53-induced glycolysis regulatory phosphataseBy similarity
Gene namesi
Name:TIGARBy similarity
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Organism-specific databases

VGNCiVGNC:35863 TIGAR

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003630661 – 270Fructose-2,6-bisphosphatase TIGARAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei50N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ1JQA7

Expressioni

Gene expression databases

BgeeiENSBTAG00000016650

Interactioni

Subunit structurei

Interacts with HK2; the interaction increases hexokinase HK2 activity in a hypoxia- and HIF1A-dependent manner, resulting in the regulation of mitochondrial membrane potential, thus increasing NADPH production and decreasing intracellular ROS levels.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022146

Structurei

3D structure databases

ProteinModelPortaliQ1JQA7
SMRiQ1JQA7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

eggNOGiENOG410IUDB Eukaryota
COG0406 LUCA
GeneTreeiENSGT00390000013224
HOGENOMiHOG000060277
HOVERGENiHBG108569
InParanoidiQ1JQA7
KOiK14634
OMAiNFEEGRE
OrthoDBiEOG091G0W1L
TreeFamiTF329053

Family and domain databases

CDDicd07067 HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
InterProiView protein in InterPro
IPR013078 His_Pase_superF_clade-1
IPR029033 His_PPase_superfam
IPR001345 PG/BPGM_mutase_AS
PfamiView protein in Pfam
PF00300 His_Phos_1, 1 hit
SMARTiView protein in SMART
SM00855 PGAM, 1 hit
SUPFAMiSSF53254 SSF53254, 2 hits
PROSITEiView protein in PROSITE
PS00175 PG_MUTASE, 1 hit

Sequencei

Sequence statusi: Complete.

Q1JQA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRFALTVVR HGETRLNKEK IIQGQGIDEP LSETGFKQAA AAGIFLKDVK
60 70 80 90 100
FTHVFSSDLT RTKQTVHGIL EKSKFCKDMT VKYDSRLRER KYGVAEGRPL
110 120 130 140 150
SELRAMAKAA GEECPAFTPP GGETLDQLKR RGKDFFEFLC QLILKEAGQN
160 170 180 190 200
EQFSQEAPSS CLESSLAEIF PLGKNCASTF NSDSGTPGLA ASVLVVSHGA
210 220 230 240 250
YIRSLLDYFL TDLKCSFPAT LSRSELTSVS PNTGMTVFIL NFEKGGKGRP
260 270
TAQCVCVNLQ GHLAGVNKTP
Length:270
Mass (Da):29,467
Last modified:June 13, 2006 - v1
Checksum:i2D738CBE454EA6D8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC116101 mRNA Translation: AAI16102.1
RefSeqiNP_001069838.1, NM_001076370.1
UniGeneiBt.61374

Genome annotation databases

EnsembliENSBTAT00000022146; ENSBTAP00000022146; ENSBTAG00000016650
GeneIDi615392
KEGGibta:615392

Similar proteinsi

Entry informationi

Entry nameiTIGAR_BOVIN
AccessioniPrimary (citable) accession number: Q1JQA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: June 13, 2006
Last modified: March 28, 2018
This is version 74 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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