GLRX3

Protein-coding gene in the species Homo sapiens
GLRX3
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2DIY, 2WZ9, 2YAN, 3ZYW

Identifiers
AliasesGLRX3, GLRX4, GRX3, GRX4, PICOT, TXNL2, TXNL3, glutaredoxin 3
External IDsOMIM: 612754; MGI: 1353653; HomoloGene: 4769; GeneCards: GLRX3; OMA:GLRX3 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for GLRX3
Genomic location for GLRX3
Band10q26.3Start130,136,391 bp[1]
End130,184,521 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for GLRX3
Genomic location for GLRX3
Band7|7 F4Start137,039,343 bp[2]
End137,070,323 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • islet of Langerhans

  • right testis

  • left testis

  • mucosa of esophagus

  • right adrenal gland

  • right adrenal cortex

  • left adrenal gland

  • left adrenal cortex

  • body of pancreas
Top expressed in
  • spermatid

  • spermatocyte

  • yolk sac

  • ankle joint

  • corneal stroma

  • plantaris muscle

  • entorhinal cortex

  • extensor digitorum longus muscle

  • morula

  • superior frontal gyrus
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • protein-disulfide reductase activity
  • electron transfer activity
  • iron-sulfur cluster binding
  • protein binding
  • metal ion binding
  • protein kinase C binding
  • RNA binding
  • identical protein binding
  • glutathione disulfide oxidoreductase activity
Cellular component
  • cytoplasm
  • dendrite
  • cell cortex
  • Z disc
  • extracellular exosome
  • nucleus
  • cytosol
Biological process
  • cell redox homeostasis
  • negative regulation of cardiac muscle hypertrophy
  • regulation of the force of heart contraction
  • [2Fe-2S cluster assembly]
  • protein maturation by iron-sulfur cluster transfer
  • electron transport chain
  • cellular iron ion homeostasis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10539

30926

Ensembl

ENSG00000108010

ENSMUSG00000031068

UniProt

O76003

Q9CQM9

RefSeq (mRNA)

NM_001199868
NM_006541
NM_001321980

NM_023140
NM_001348093

RefSeq (protein)

NP_001186797
NP_001308909
NP_006532

NP_075629
NP_001335022

Location (UCSC)Chr 10: 130.14 – 130.18 MbChr 7: 137.04 – 137.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Glutaredoxin-3 is a protein that in humans is encoded by the GLRX3 gene.[5][6][7]

Interactions

GLRX3 has been shown to interact with PRKCQ.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000108010 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031068 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Witte S, Villalba M, Bi K, Liu Y, Isakov N, Altman A (Feb 2000). "Inhibition of the c-Jun N-terminal kinase/AP-1 and NF-kappaB pathways by PICOT, a novel protein kinase C-interacting protein with a thioredoxin homology domain". J Biol Chem. 275 (3): 1902–9. doi:10.1074/jbc.275.3.1902. PMID 10636891.
  6. ^ Stanchi F, Bertocco E, Toppo S, Dioguardi R, Simionati B, Cannata N, Zimbello R, Lanfranchi G, Valle G (Jan 2001). "Characterization of 16 novel human genes showing high similarity to yeast sequences". Yeast. 18 (1): 69–80. doi:10.1002/1097-0061(200101)18:1<69::AID-YEA647>3.0.CO;2-H. PMID 11124703. S2CID 21397515.
  7. ^ "Entrez Gene: TXNL2 thioredoxin-like 2".

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links

  • Overview of all the structural information available in the PDB for UniProt: O76003 (Human Glutaredoxin-3 (GLRX3)) at the PDBe-KB.


  • v
  • t
  • e
  • 1wik: Solution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein
    1wik: Solution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein
  • 2diy: The solution structure of the thioredoxin domain of human Thioredoxin-like protein 2
    2diy: The solution structure of the thioredoxin domain of human Thioredoxin-like protein 2
  • v
  • t
  • e
Other oxidoreductases (EC 1.15–1.21)
1.15: Acting on superoxide as acceptor
1.16: Oxidizing metal ions
1.17: Acting on CH or CH2 groups
1.18: Acting on iron–sulfur proteins as donors
1.19: Acting on reduced flavodoxin as donor
  • Nitrogenase (flavodoxin)
1.20: Acting on phosphorus or arsenic in donors
1.21: Acting on X-H and Y-H to form an X-Y bond


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