SUMO2

From Wikipedia, the free encyclopedia

SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)

PDB rendering based on 1u4a.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1WM2, 1WM3, 1WZ0, 2AWT, 2CKH, 2D07, 2IO0, 2IO3, 2IYD, 2RPQ, 3UIN, 3UIO, 4BKG

Identifiers

Symbols

SUMO2; HSMT3; SMT3B; SMT3H2; SUMO3; Smt3A

External IDs

OMIM: 603042 MGI: 2158813 HomoloGene: 87858 GeneCards: SUMO2 Gene

Gene Ontology
Molecular function	• protein binding • ubiquitin protein ligase binding
Cellular component	• PML body
Biological process	• protein sumoylation • positive regulation of proteasomal ubiquitin-dependent protein catabolic process
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 17:
73.16 – 73.18 Mb

Chr 11:
115.52 – 115.54 Mb

PubMed search

Small ubiquitin-related modifier 2 is a protein that in humans is encoded by the SUMO2 gene.^[1]

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.^[2]

Interactions

SUMO2 has been shown to interact with TRIM63^[3] and c21orf59.^[4]

References

↑ Mannen H, Tseng HM, Cho CL, Li SS (June 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.
↑ "Entrez Gene: SUMO2 SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)".
↑ Dai, K S; Liew C C (June 2001). "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain". J. Biol. Chem. (United States) 276 (26): 23992–9. doi:10.1074/jbc.M011208200. ISSN 0021-9258. PMID 11283016. Cite uses deprecated parameters (help)
↑ Golebiowski, F.; Matic, I.; Tatham, M. H.; Cole, C.; Yin, Y.; Nakamura, A.; Cox, J.; Barton, G. J.; Mann, M.; Hay, R. T. (2009). "System-Wide Changes to SUMO Modifications in Response to Heat Shock". Science Signaling 2 (72): ra24. doi:10.1126/scisignal.2000282. PMID 19471022.

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.
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. doi:10.1016/S0378-1119(97)00411-3. 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. doi:10.1074/jbc.273.6.3117. 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. doi:10.1074/jbc.273.18.11349. 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. doi:10.1074/jbc.275.9.6252. 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. doi:10.1046/j.1432-1327.2000.01729.x. 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. PMC 125358. 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. 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.
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. doi:10.1128/MCB.23.8.2953-2968.2003. PMC 152542. 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.

PDB gallery

1u4a: Solution structure of human SUMO-3 C47S

1wm2: Crystal structure of human SUMO-2 protein

1wm3: Crystal structure of human SUMO-2 protein

1wz0: Solution Structure of Human SUMO-2 (SMT3B), a Ubiquitin-like Protein

2awt: Solution Structure of Human Small Ubiquitin-Like Modifier Protein Isoform 2 (SUMO-2)

2ckh: SENP1-SUMO2 COMPLEX

2d07: Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase

2io0: Crystal structure of human Senp2 in complex with preSUMO-2

2io1: Crystal structure of human Senp2 in complex with preSUMO-3

2io3: Crystal structure of human Senp2 in complex with RanGAP1-SUMO-2

2iyd: SENP1 COVALENT COMPLEX WITH SUMO-2

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SUMO2

Interactions

References

Further reading