SUMO3

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SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)
File:PBB Protein SUMO3 image.jpg
PDB rendering based on 1u4a.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols SUMO3 ; SMT3A; SMT3H1; SUMO-3
External IDs Template:OMIM5 Template:MGI HomoloGene: 38251
RNA expression pattern
File:PBB GE SUMO3 200740 s at tn.png
File:PBB GE SUMO3 200739 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae), also known as SUMO3, is a human gene.[1]

SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002).[supplied by OMIM][1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)".

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. PMID 8125298.
  • Lapenta V, Chiurazzi P, van der Spek P; et al. (1997). "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family". Genomics. 40 (2): 362–6. doi:10.1006/geno.1996.4556. PMID 9119407.
  • 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. PMID 9373149.
  • Saitoh H, Hinchey J (2000). "Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3". J. Biol. Chem. 275 (9): 6252–8. PMID 10692421.
  • Hattori M, Fujiyama A, Taylor TD; et al. (2000). "The DNA sequence of human chromosome 21". Nature. 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
  • Tatham MH, Jaffray E, Vaughan OA; et al. (2001). "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9". J. Biol. Chem. 276 (38): 35368–74. doi:10.1074/jbc.M104214200. PMID 11451954.
  • Lin J, Johannsen E, Robertson E, Kieff E (2002). "Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2". J. Virol. 76 (1): 232–42. PMID 11739688.
  • Kadoya T, Yamamoto H, Suzuki T; et al. (2002). "Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin". Mol. Cell. Biol. 22 (11): 3803–19. PMID 11997515.
  • Su HL, Li SS (2003). "Molecular features of human ubiquitin-like SUMO genes and their encoded proteins". Gene. 296 (1–2): 65–73. PMID 12383504.
  • 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. doi:10.1073/pnas.242603899. PMID 12477932.
  • Subramanian L, Benson MD, Iñiguez-Lluhí JA (2003). "A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3". J. Biol. Chem. 278 (11): 9134–41. doi:10.1074/jbc.M210440200. PMID 12511558.
  • Eaton EM, Sealy L (2003). "Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3". J. Biol. Chem. 278 (35): 33416–21. doi:10.1074/jbc.M305680200. PMID 12810706.
  • Tatham MH, Kim S, Yu B; et al. (2003). "Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation". Biochemistry. 42 (33): 9959–69. doi:10.1021/bi0345283. PMID 12924945.
  • Dobreva G, Dambacher J, Grosschedl R (2004). "SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression". Genes Dev. 17 (24): 3048–61. doi:10.1101/gad.1153003. PMID 14701874.
  • Reverter D, Lima CD (2005). "A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex". Structure. 12 (8): 1519–31. doi:10.1016/j.str.2004.05.023. PMID 15296745.
  • Ayaydin F, Dasso M (2005). "Distinct in vivo dynamics of vertebrate SUMO paralogues". Mol. Biol. Cell. 15 (12): 5208–18. doi:10.1091/mbc.E04-07-0589. PMID 15456902.
  • Xu Z, Au SW (2005). "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1". Biochem. J. 386 (Pt 2): 325–30. doi:10.1042/BJ20041210. PMID 15487983.
  • 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. PMID 15489334.
  • Ding H, Xu Y, Chen Q; et al. (2005). "Solution structure of human SUMO-3 C47S and its binding surface for Ubc9". Biochemistry. 44 (8): 2790–9. doi:10.1021/bi0477586. PMID 15723523.
  • Bossis G, Malnou CE, Farras R; et al. (2005). "Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation". Mol. Cell. Biol. 25 (16): 6964–79. doi:10.1128/MCB.25.16.6964-6979.2005. PMID 16055710.

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