SUMO2

SUMO2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1WM2, 1WM3, 1WZ0, 2AWT, 2CKH, 2D07, 2IO0, 2IO3, 2IYD, 2RPQ, 3UIN, 3UIO, 3ZO5, 4BKG, 4NPN, 2N9E, 5D2M, 2N1W
Identifiers
Aliases	SUMO2, HSMT3, SMT3B, SMT3H2, SUMO3, Smt3A, small ubiquitin-like modifier 2, small ubiquitin like modifier 2
External IDs	OMIM: 603042 MGI: 2158813 HomoloGene: 87858 GeneCards: SUMO2
Gene location (Human)
Chr.	Chromosome 17 (human)[1]
End	75,182,959 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	115,536,276 bp[2]
Gene ontology
Molecular function	• GO:0001948 protein binding; • ubiquitin protein ligase binding; • protein tag; • RNA binding; • transcription corepressor binding; • SUMO transferase activity; • ubiquitin-like protein ligase binding;
Cellular component	• PML body; • cell nucleus; • nucleoplasm;
Biological process	• global genome nucleotide-excision repair; • positive regulation of proteasomal ubiquitin-dependent protein catabolic process; • protein sumoylation; • positive regulation of transcription from RNA polymerase II promoter;
	Sources:Amigo / QuickGO
Orthologs
	6613
	170930
	ENSG00000188612
	ENSMUSG00000020738
	P61956
	P61957
	NM_001005849; NM_006937
	NM_133354
	NP_001005849; NP_008868
	NP_579932
	Wikidata
View/Edit Human	View/Edit Mouse

Small ubiquitin-related modifier 2 is a protein that in humans is encoded by the SUMO2 gene.[5]

Function

This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It is a ubiquitin-like protein and 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 is primarily associated with targeting proteins for proteasomal degradation, SUMO2 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.[6]

Interactions

SUMO2 has been shown to interact with TRIM63[7] and CFAP298.[8]

References

GRCh38: Ensembl release 89: ENSG00000188612 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000020738 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Mannen H, Tseng HM, Cho CL, Li SS (May 1996). "Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene". Biochemical and Biophysical Research Communications. 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 KS, Liew CC (Jun 2001). "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain". The Journal of Biological Chemistry. 276 (26): 23992–9. doi:10.1074/jbc.M011208200. PMID 11283016.
Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT (2009). "System-wide changes to SUMO modifications in response to heat shock". Science Signaling. 2 (72): ra24. doi:10.1126/scisignal.2000282. PMID 19471022. S2CID 33450256.

Maruyama K, Sugano S (Jan 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, Pizzuti A, Hanaoka F, Brahe C (Mar 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, Suyama A, Sugano S (Oct 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, Fukuda-Kamitani T, Yeh ET (Feb 1998). "Covalent modification of PML by the sentrin family of ubiquitin-like proteins". The Journal of Biological Chemistry. 273 (6): 3117–20. doi:10.1074/jbc.273.6.3117. PMID 9452416.
Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET (May 1998). "Characterization of a second member of the sentrin family of ubiquitin-like proteins". The Journal of Biological Chemistry. 273 (18): 11349–53. doi:10.1074/jbc.273.18.11349. PMID 9556629.
Saitoh H, Hinchey J (Mar 2000). "Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3". The Journal of Biological Chemistry. 275 (9): 6252–8. doi:10.1074/jbc.275.9.6252. PMID 10692421.
Nishida T, Tanaka H, Yasuda H (Nov 2000). "A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase". European Journal of Biochemistry / FEBS. 267 (21): 6423–7. doi:10.1046/j.1432-1327.2000.01729.x. PMID 11029585.
Dai KS, Liew CC (Jun 2001). "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain". The Journal of Biological Chemistry. 276 (26): 23992–9. doi:10.1074/jbc.M011208200. PMID 11283016.
Tatham MH, Jaffray E, Vaughan OA, Desterro JM, Botting CH, Naismith JH, Hay RT (Sep 2001). "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9". The Journal of Biological Chemistry. 276 (38): 35368–74. doi:10.1074/jbc.M104214200. PMID 11451954.
Nishida T, Kaneko F, Kitagawa M, Yasuda H (Oct 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". The Journal of Biological Chemistry. 276 (42): 39060–6. doi:10.1074/jbc.M103955200. PMID 11489887.
Hardeland U, Steinacher R, Jiricny J, Schär P (Mar 2002). "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover". The EMBO Journal. 21 (6): 1456–64. doi:10.1093/emboj/21.6.1456. PMC 125358. PMID 11889051.
Kim J, Cantwell CA, Johnson PF, Pfarr CM, Williams SC (Oct 2002). "Transcriptional activity of CCAAT/enhancer-binding proteins is controlled by a conserved inhibitory domain that is a target for sumoylation". The Journal of Biological Chemistry. 277 (41): 38037–44. doi:10.1074/jbc.M207235200. PMID 12161447.
Su HL, Li SS (Aug 2002). "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.
Petrie K, Guidez F, Howell L, Healy L, Waxman S, Greaves M, Zelent A (May 2003). "The histone deacetylase 9 gene encodes multiple protein isoforms". The Journal of Biological Chemistry. 278 (18): 16059–72. doi:10.1074/jbc.M212935200. PMID 12590135.
Hietakangas V, Ahlskog JK, Jakobsson AM, Hellesuo M, Sahlberg NM, Holmberg CI, Mikhailov A, Palvimo JJ, Pirkkala L, Sistonen L (Apr 2003). "Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1". Molecular and Cellular Biology. 23 (8): 2953–68. doi:10.1128/MCB.23.8.2953-2968.2003. PMC 152542. PMID 12665592.
Eaton EM, Sealy L (Aug 2003). "Modification of CCAAT/enhancer-binding protein-beta by the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3". The Journal of Biological Chemistry. 278 (35): 33416–21. doi:10.1074/jbc.M305680200. PMID 12810706.
Tatham MH, Kim S, Yu B, Jaffray E, Song J, Zheng J, Rodriguez MS, Hay RT, Chen Y (Aug 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, Shia HL, Chen YL, Liang PH, Wang AH, Khoo KH, Shoei-Lung Li S (Sep 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". The Journal of Biological Chemistry. 279 (38): 39653–62. doi:10.1074/jbc.M405637200. PMID 15272016.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000188612 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020738 - 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.

[pmid8630065-5] Mannen H, Tseng HM, Cho CL, Li SS (May 1996). "Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene". Biochemical and Biophysical Research Communications. 222 (1): 178–80. doi:10.1006/bbrc.1996.0717. PMID 8630065.

[entrez-6] "Entrez Gene: SUMO2 SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)".

[pmid11283016-7] Dai KS, Liew CC (Jun 2001). "A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain". The Journal of Biological Chemistry. 276 (26): 23992–9. doi:10.1074/jbc.M011208200. PMID 11283016.

[pmid19471022-8] Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT (2009). "System-wide changes to SUMO modifications in response to heat shock". Science Signaling. 2 (72): ra24. doi:10.1126/scisignal.2000282. PMID 19471022. S2CID 33450256.

SUMO2

Function

Interactions

References

Further reading