SUMO2

Protein-coding gene in the species Homo sapiens

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; OMA:SUMO2 - orthologs

Gene location (Human)

Chr.	Chromosome 17 (human)^[1]

Band	17q25.1	Start	75,165,586 bp^[1]
Band	17q25.1	End	75,182,959 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 11 (mouse)^[2]

Band	11\|11 E2	Start	115,413,928 bp^[2]
Band	11\|11 E2	End	115,427,102 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

ganglionic eminence

ventricular zone

mucosa of paranasal sinus

endothelial cell

lower lobe of lung

superficial temporal artery

islet of Langerhans

cerebellar vermis

oocyte

monocyte

Top expressed in

tail of embryo

morula

neural tube

mesencephalon

epiblast

ganglionic eminence

embryo

ventricular zone

genital tubercle

ovary

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	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 nucleus nucleoplasm
Biological process	global genome nucleotide-excision repair positive regulation of proteasomal ubiquitin-dependent protein catabolic process protein sumoylation positive regulation of transcription by RNA polymerase II
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


6613


170930

Ensembl


ENSG00000188612


ENSMUSG00000020738

UniProt


P61956


P61957

RefSeq (mRNA)


NM_001005849 NM_006937


NM_133354

RefSeq (protein)


NP_001005849 NP_008868


NP_579932

Location (UCSC)

Chr 17: 75.17 – 75.18 Mb

Chr 11: 115.41 – 115.43 Mb

PubMed search

^[3]

^[4]

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]

Clinical significance

Deep hypothermia protects the brain from ischemic injury, which is why it's employed for major cardiovascular procedures that necessitate cardiopulmonary bypass and a period of circulatory arrest. With an experiment ^[9] conducted to moderate hypothermia, small ubiquitin-like modifier (SUMO1-3) conjugation was significantly activated in the brain. The effects of hypothermia on SUMO conjugation were evaluated in this experiment^[9] using Western blot and immunohistochemistry in animals that were either normothermic (37 °C) or deep to moderate (18 °C, 24 °C, 30 °C) hypothermic cardiopulmonary bypass. In these cells, even 30 °C hypothermia was enough to significantly boost SUMO2/3-conjugated protein levels and nucleus accumulation. Deep hypothermia caused the SUMO-conjugating enzyme Ubc9 to translocate to the nucleus, implying that the increase in nuclear levels of SUMO2/3-conjugated proteins seen in hypothermic animals' brains is an active process. Deep hypothermia caused only a small increase in the amounts of SUMO2/3-conjugated proteins in primary neuronal cells. This shows that neurons in vivo have a greater capacity to activate this endogenous possibly neuroprotective mechanism when exposed to hypothermia than neurons in vitro. Identifying proteins that are SUMO2/3 conjugated during hypothermia could aid in the development of new preventive and therapeutic therapies to make neurons more resistant to a transient blood supply interruption.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000188612 – Ensembl, May 2017
^ ^a ^b ^c 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.
^ ^a ^b Wang, Liangli; Ma, Qing; Yang, Wei; Mackensen, G. Burkhard; Paschen, Wulf (November 2012). "Moderate hypothermia induces marked increase in levels and nuclear accumulation of SUMO2/3-conjugated proteins in neurons". Journal of Neurochemistry. 123 (3): 349–359. doi:10.1111/j.1471-4159.2012.07916.x. PMC 3466336. PMID 22891650.

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. 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.

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