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SH3BGRL3

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SH3BGRL3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSH3BGRL3, HEL-S-297, SH3BP-1, TIP-B1, SH3 domain binding glutamate rich protein like 3
External IDsOMIM: 615679; MGI: 1920973; HomoloGene: 41824; GeneCards: SH3BGRL3; OMA:SH3BGRL3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_031286

NM_080559

RefSeq (protein)

NP_112576

NP_542126

Location (UCSC)Chr 1: 26.28 – 26.28 MbChr 4: 133.85 – 133.86 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

SH3 domain-binding glutamic acid-rich-like protein 3 is a protein that in humans is encoded by the SH3BGRL3 gene.[5]

The 10.5kDa protein SH3 binding glutamic acid-rich protein-like 3 has an isoelectric point of 5.0. SH3 binding glutamic acid-rich (SH3BGR) gene is located to human chromosome 21. Two homologous genes, SH3BGRL and SH3BGRL3 are located to chromosome Xq13.3 and 1p34.3-35, respectively and code for small proteins similar to the N-terminal region of the SH3BGR protein.[6] SH3BGRL3 protein shows a significant similarity to glutaredoxin 1 of E. coli, and all the three proteins are predicted to belong to thioredoxin-like protein family. Glutaredoxins (GRXs) are ubiquitous oxidoreductases, which catalyze the reduction of many intra-cellular protein disulfides and play an important role in many redox pathways. However, the SH3BGRL3 protein lacks the enzymatic function of glutaredoxins and may have a role as a regulator of redox activity.[7]

Role in cancer

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Proteins such as glutaredoxin and thioredoxin are reported as up-regulated in many cancers such as lung and pancreatic; they have been implicated in increased resistance of cancer cells to free-radicals. There is little current evidence which directly links SH3GRPL3 with survival in cancer cells, however the protein has recently been identified as up-regulated in glioblastoma multiforme compared to normal cerebral tissue on proteomic analysis.[8] Studies of acute promyelocytic leukemia cell line NB4 have also reported up-regulation of the protein. Conversely, the related protein SH3BGRL is reported to be downregulated in fibroblasts, lymphoid cells, and splenic tumor cells transformed by the viral oncogene v-Rel.[9] Co-expression of SH3BGRL with v-Rel in primary splenic lymphocytes reduced the number of colonies formed by 76%. Xu et al. reported SH3BGRPL3 protein as a post-translational modification of the 27kDa tumor necrosis factor alpha (TNF-α) inhibitory protein, TIP-B1. This protein is potentially involved in resistance of cells to the apoptosis-inducing effect of TNF-α.[10]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000142669Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028843Ensembl, 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. ^ "Entrez Gene: SH3BGRL3 SH3 domain binding glutamic acid-rich protein like 3".
  6. ^ Egeo A, Mazzocco M, Arrigo P, Vidal-Taboada JM, Oliva R, Pirola B, Giglio S, Rasore-Quartino A, Scartezzini P (June 1998). "Identification and characterization of a new human gene encoding a small protein with high homology to the proline-rich region of the SH3BGR gene". Biochem. Biophys. Res. Commun. 247 (2): 302–6. doi:10.1006/bbrc.1998.8763. PMID 9642120.
  7. ^ Mazzocco M, Maffei M, Egeo A, Vergano A, Arrigo P, Di Lisi R, Ghiotto F, Scartezzini P (May 2002). "The identification of a novel human homologue of the SH3 binding glutamic acid-rich (SH3BGR) gene establishes a new family of highly conserved small proteins related to Thioredoxin Superfamily". Gene. 291 (1–2): 233–9. doi:10.1016/S0378-1119(02)00602-9. PMID 12095696.
  8. ^ Khalil AA, James P (February 2007). "Biomarker discovery: a proteomic approach for brain cancer profiling". Cancer Sci. 98 (2): 201–13. doi:10.1111/j.1349-7006.2007.00374.x. PMC 11158801. PMID 17233837.
  9. ^ Majid SM, Liss AS, You M, Bose HR (February 2006). "The suppression of SH3BGRL is important for v-Rel-mediated transformation". Oncogene. 25 (5): 756–68. doi:10.1038/sj.onc.1209107. PMID 16186799.
  10. ^ Xu C, Zheng P, Shen S, Xu Y, Wei L, Gao H, Wang S, Zhu C, Tang Y, Wu J, Zhang Q, Shi Y (May 2005). "NMR structure and regulated expression in APL cell of human SH3BGRL3". FEBS Lett. 579 (13): 2788–94. doi:10.1016/j.febslet.2005.04.011. PMID 15907482.

Further reading

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