SH3BGRL3

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

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
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1p36.11Start26,280,086 bp[1]
End26,281,522 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

83442

73723

Ensembl

ENSG00000142669

ENSMUSG00000028843

UniProt

Q9H299

Q91VW3

RefSeq (mRNA)

NM_031286

NM_080559

RefSeq (protein)

NP_112576

NP_542126

Location (UCSC)Chr 1: 26.28 – 26.28 MbChr 4: 134.13 – 134.13 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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

  1. GRCh38: Ensembl release 89: ENSG00000142669 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000028843 - 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. "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. 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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