SUMO3

Small ubiquitin-like modifier 3
PDB rendering based on 1u4a.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1U4A​, 2IO1​, 2MP2​
Identifiers
Symbols	SUMO3 ; SMT3A; SMT3H1; SUMO-3; Smt3B
External IDs	OMIM: 602231 MGI: 1336201 HomoloGene: 38251 GeneCards: SUMO3 Gene
Gene ontology Molecular function • protein binding • SUMO transferase activity Cellular component • kinetochore • nucleus • nucleoplasm • cytoplasm • PML body • extracellular exosome Biological process • protein sumoylation • protein localization to nucleus • post-translational protein modification • cellular protein metabolic process • positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6612	20610
Ensembl	ENSG00000184900	ENSMUSG00000020265
UniProt	P55854	Q9Z172
RefSeq (mRNA)	NM_001286416	NM_001301671
RefSeq (protein)	NP_001273345	NP_001288600
Location (UCSC)	Chr 21: 44.81 – 44.82 Mb	Chr 10: 77.61 – 77.64 Mb
PubMed search

Small ubiquitin-related modifier 3 is a protein that in humans is encoded by the SUMO3 gene.^[1][2]

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]^[2]

Interactions

SUMO3 has been shown to interact with ARNTL^[3] and Thymine-DNA glycosylase.^[4]

References

1. Lapenta V, Chiurazzi P, van der Spek P, Pizzuti A, Hanaoka F, Brahe C (Apr 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.
2. "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)".
3. Lee, Jiwon; Lee Yool; Lee Min Joo; Park Eonyoung; Kang Sung Hwan; Chung Chin Ha; Lee Kun Ho; Kim Kyungjin (Oct 2008). "Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex". Mol. Cell. Biol. (United States) 28 (19): 6056–65. doi:10.1128/MCB.00583-08. PMC 2546997. PMID 18644859.
4. Hardeland, Ulrike; Steinacher Roland; Jiricny Josef; Schär Primo (Mar 2002). "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover". EMBO J. (England) 21 (6): 1456–64. doi:10.1093/emboj/21.6.1456. ISSN 0261-4189. PMC 125358. PMID 11889051.

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.
• 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. doi:10.1074/jbc.275.9.6252. 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. doi:10.1128/JVI.76.1.232-242.2002. PMC 135708. 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. doi:10.1128/MCB.22.11.3803-3819.2002. PMC 133821. 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. doi:10.1016/S0378-1119(02)00843-0. 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. PMC 139241. 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. PMC 305257. 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. PMC 532004. 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. PMC 1134797. 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. PMC 528928. 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. PMC 1190241. PMID 16055710.