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0GLRX2_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGLRX2
DescriptionGlutaredoxin-2, mitochondrial precursor.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005739 mitochondrion (IDA)
0005634 nucleus (IEP)
0008794 arsenate reductase (glutaredoxin) activity (TAS)
0009053 electron donor activity (NAS)
0015038 glutathione disulfide oxidoreductase activity (TAS)
0030508 thiol-disulfide exchange intermediate activity (TAS)
0006915 apoptosis (NAS)
0030154 cell differentiation (NAS)
0042262 DNA protection (NAS)
0006749 glutathione metabolism (TAS)
0006467 protein thiol-disulfide exchange (TAS)
0006980 redox signal response (TAS)
0030503 regulation of cell redox homeostasis (TAS)
0009966 regulation of signal transduction (NAS)
0045449 regulation of transcription (NAS)
0042542 response to hydrogen peroxide (IDA)
0010033 response to organic substance (IDA)
0009268 response to pH (IDA)
0009266 response to temperature (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2).here a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system.he NADP/thioredoxin system.nd the glutathione/glutaredoxin system . Several of these disulphide proteins share a common structure.onsisting of a three-layer alpha/beta/alpha core. Proteins that contain this thioredoxin fold include: 2Fe-2S ferredoxin.hioltransferase.hosducin.lutathione peroxidase-like enzymes.rsenate reductase.isulphide bond isomerase DsbC (C-terminal domain).isulphide bond facilitator DsbA (contains an alpha-helical insertion).lutathione S-transferase (N-terminal domain).ndoplasmic reticulum protein ERP29 (N-terminal domain).pliceosomal protein U5-15Kd.ircadian oscillation regulator KaiB.rotein disulphide isomerase PDI (contains two tandem repeats of this fold).nd calsequestrin (contains three tandem repeats of this fold).This entry differs from the thioredoxin-like fold protein.he classification of this fold in glutathione S-transferase enzymes.here this entry defines two regions containing this fold.nd the thioredoxin-like fold protein defines only the N-terminal as containing this fold.
  IPR012335:Thioredoxin fold
Glutaredoxins .lso known as thioltransferases.re small proteins of approximately one hundred amino-acid residues. Glutaredoxin functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. Like thioredoxin.hich functions in a similar way.lutaredoxin possesses an active center disulphide bond. It exists in either a reduced or an oxidized form where the two cysteine residues are linked in an intramolecular disulphide bond.Glutaredoxin has been sequenced in a variety of species. On the basis of extensive sequence similarity.t has been proposed that vaccinia protein O2L is most probably a glutaredoxin. Finally.t must be noted that phage T4 thioredoxin seems also to be evolutionary related.
  IPR002109:Glutaredoxin
Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system . Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress.eduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides.Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system . Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress.eduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family represents eukaryotic glutaredoxins and includes sequences from fungi.lants and metazoans as well as viruses .
  IPR011899:Glutaredoxin, eukaryotic and viruses
Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2).here a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system.he NADP/thioredoxin system.nd the glutathione/glutaredoxin system . Several of these disulphide proteins share a common structure.onsisting of a three-layer alpha/beta/alpha core. Proteins that contain this thioredoxin fold include: 2Fe-2S ferredoxin.hioltransferase.hosducin.lutathione peroxidase-like enzymes.rsenate reductase.isulphide bond isomerase DsbC (C-terminal domain).isulphide bond facilitator DsbA (contains an alpha-helical insertion).lutathione S-transferase (N-terminal domain).ndoplasmic reticulum protein ERP29 (N-terminal domain).pliceosomal protein U5-15Kd.ircadian oscillation regulator KaiB.rotein disulphide isomerase PDI (contains two tandem repeats of this fold).nd calsequestrin (contains three tandem repeats of this fold).This entry differs from the thioredoxin fold protein.he classification of this fold is in the glutathione S-transferase enzymes.here this entry defines two regions containing this fold.nd the thioredoxin fold protein defines only the N-terminal as containing this fold.
  IPR012336:Thioredoxin-like fold
IPR012335:Thioredoxin_fold 
Evalue:-25.7958793640137 
Location:56-157IPR011767:GLUTAREDOXIN 
Evalue:0 
Location:0-0
SequencesProtein: GLRX2_HUMAN (164 aa)
mRNA: NM_197962
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 97 residues, 191332222-191332512Exon2: 61 residues, 191333336-191333513Exon3: 23 residues, 191336893-191336957Exon4: 56 residues, 191341016-191341179Exon5: 2 residues, -Jump to GLRX2_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3854 191332222-191341179 ~-9K 3563(GLRX2)(-)Loci: 3855 191414798-191422363 ~-8K 3566(B3GALT2)(-)Loci: 2577 191044793-191048026 ~-3K 3553(RGS2)(+)Link out to UCSC