SUMO2

From Wikipedia, the free encyclopedia


SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)
PDB rendering based on 1u4a.
Available structures: 1u4a, 1wm2, 1wm3, 1wz0, 2awt, 2ckh, 2d07, 2io0, 2io1, 2io3, 2iyd
Identifiers
Symbol(s) SUMO2; HSMT3; MGC117191; SMT3B; SMT3H2
External IDs OMIM: 603042 MGI: 2158813 HomoloGene: 87858
Orthologs
Human Mouse
Entrez 6613 170930
Ensembl n/a ENSMUSG00000020738
Uniprot n/a P61957
Refseq NM_001005849 (mRNA)
NP_001005849 (protein)		 NM_133354 (mRNA)
NP_579932 (protein)
Location n/a Chr 11: 115.34 - 115.35 Mb
Pubmed search [1] [2]

SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae), also known as SUMO2, is a human gene.

This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last two amino acids of the carboxy-terminus have been cleaved off. Numerous pseudogenes have been reported for this gene. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[1]

[edit] References

  1. ^ Entrez Gene: SUMO2 SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae).

[edit] 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. 
  • Mannen H, Tseng HM, Cho CL, Li SS (1996). "Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene.". Biochem. Biophys. Res. Commun. 222 (1): 178–80. doi:10.1006/bbrc.1996.0717. PMID 8630065. 
  • 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. 
  • Kamitani T, Nguyen HP, Kito K, et al. (1998). "Covalent modification of PML by the sentrin family of ubiquitin-like proteins.". J. Biol. Chem. 273 (6): 3117–20. PMID 9452416. 
  • Kamitani T, Kito K, Nguyen HP, et al. (1998). "Characterization of a second member of the sentrin family of ubiquitin-like proteins.". J. Biol. Chem. 273 (18): 11349–53. PMID 9556629. 
  • 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. 
  • Nishida T, Tanaka H, Yasuda H (2000). "A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase.". Eur. J. Biochem. 267 (21): 6423–7. PMID 11029585. 
  • Dai KS, Liew CC (2001). "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain.". J. Biol. Chem. 276 (26): 23992–9. doi:10.1074/jbc.M011208200. PMID 11283016. 
  • 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. 
  • Nishida T, Kaneko F, Kitagawa M, Yasuda H (2001). "Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat axam, which is an axin-binding protein promoting beta-catenin degradation.". J. Biol. Chem. 276 (42): 39060–6. doi:10.1074/jbc.M103955200. PMID 11489887. 
  • Hardeland U, Steinacher R, Jiricny J, Schär P (2002). "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover.". EMBO J. 21 (6): 1456–64. doi:10.1093/emboj/21.6.1456. PMID 11889051. 
  • Kim J, Cantwell CA, Johnson PF, et al. (2002). "Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation.". J. Biol. Chem. 277 (41): 38037–44. doi:10.1074/jbc.M207235200. PMID 12161447. 
  • 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. 
  • Petrie K, Guidez F, Howell L, et al. (2003). "The histone deacetylase 9 gene encodes multiple protein isoforms.". J. Biol. Chem. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135. 
  • Hietakangas V, Ahlskog JK, Jakobsson AM, et al. (2003). "Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1.". Mol. Cell. Biol. 23 (8): 2953–68. PMID 12665592. 
  • 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. 
  • Chung TL, Hsiao HH, Yeh YY, et al. (2004). "In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: definitive identification of the modification sites by tandem mass spectrometry analysis of the isopeptides.". J. Biol. Chem. 279 (38): 39653–62. doi:10.1074/jbc.M405637200. PMID 15272016. 
 This protein-related article is a stub. You can help Wikipedia by expanding it.