SUMO3

SUMO3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1U4A, 2IO1, 2MP2
Identifiers
Aliases	SUMO3 , SMT3A, SMT3H1, SUMO-3, Smt3B, small ubiquitin-like modifier 3, small ubiquitin like modifier 3
External IDs	OMIM: 602231 MGI: 1336201 HomoloGene: 38251 GeneCards: SUMO3
Gene location (Human)
Chr.	Chromosome 21 (human)
End	44,818,779 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	77,454,165 bp
RNA expression pattern
	Top expressed in
	endothelial cell; ; tibia; ; parietal pleura; ; visceral pleura; ; palpebral conjunctiva; ; germinal epithelium; ; middle temporal gyrus; ; retinal pigment epithelium; ; Brodmann area 23; ; hair follicle;
	Top expressed in
	yolk sac; ; olfactory bulb; ; mesencephalon; ; rhombencephalon; ; stomach; ; cerebellum; ; neural tube; ; urinary bladder; ; ganglionic eminence; ; superior frontal gyrus;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	protein binding ; protein tag ; enzyme binding ; ubiquitin-like protein ligase binding ;
Cellular component	cytoplasm ; PML body ; nucleus ; kinetochore ; nucleoplasm ;
Biological process	negative regulation of DNA binding ; protein sumoylation ;
	Sources:Amigo / QuickGO
Orthologs
	6612
	20610
	ENSG00000184900
	ENSMUSG00000020265
	P55854
	Q9Z172
	NM_006936 ; NM_001286416
	NM_001301671 ; NM_001301672 ; NM_001301673 ; NM_019929
	NP_001273345 ; NP_008867
	NP_001288600 ; NP_001288601 ; NP_001288602 ; NP_064313
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 16, 2023

Small ubiquitin-related modifier 3 is a protein that in humans is encoded by the SUMO3 gene.^[5]^[6]

Function

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]^[6]

Interactions

SUMO3 has been shown to interact with ARNTL ^[7] and Thymine-DNA glycosylase.^[8]

Related Research Articles

Transcription factor Sp1, also known as specificity protein 1* is a protein that in humans is encoded by the SP1 gene.

In molecular biology, SUMOproteins are a family of small proteins that are covalently attached to and detached from other proteins in cells to modify their function. This process is called SUMOylation. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.

Small ubiquitin-related modifier 1 is a protein that in humans is encoded by the SUMO1 gene.

Promyelocytic leukemia protein (PML) is the protein product of the PML gene. PML protein is a tumor suppressor protein required for the assembly of a number of nuclear structures, called PML-nuclear bodies, which form amongst the chromatin of the cell nucleus. These nuclear bodies are present in mammalian nuclei, at about 1 to 30 per cell nucleus. PML-NBs are known to have a number of regulatory cellular functions, including involvement in programmed cell death, genome stability, antiviral effects and controlling cell division. PML mutation or loss, and the subsequent dysregulation of these processes, has been implicated in a variety of cancers.

Transcription factor 3, also known as TCF3, is a protein that in humans is encoded by the TCF3 gene. TCF3 has been shown to directly enhance Hes1 expression.

SUMO-conjugating enzyme UBC9 is an enzyme that in humans is encoded by the UBE2I gene. It is also sometimes referred to as "ubiquitin conjugating enzyme E2I" or "ubiquitin carrier protein 9", even though these names do not accurately describe its function.

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

Ribosomal protein S6 kinase alpha-1 is an enzyme that in humans is encoded by the RPS6KA1 gene.

General transcription factor II-I is a protein that in humans is encoded by the GTF2I gene.

Ran GTPase-activating protein 1 is an enzyme that in humans is encoded by the RANGAP1 gene.

CDC34 is a gene that in humans encodes the protein Ubiquitin-conjugating enzyme E2 R1. This protein is a member of the ubiquitin-conjugating enzyme family, which catalyzes the covalent attachment of ubiquitin to other proteins.

E3 ubiquitin-protein ligase SIAH2 is an enzyme that in humans is encoded by the SIAH2 gene.

Nuclear transcription factor Y subunit gamma is a protein that in humans is encoded by the NFYC gene.

Lysine-specific demethylase 5A is an enzyme that in humans is encoded by the KDM5A gene.

SUMO-activating enzyme subunit 1 is a protein that in humans is encoded by the SAE1 gene.

SUMO1/sentrin/SMT3 specific peptidase 3, also known as SENP3, is a protein which in humans is encoded by the SENP3 gene.

Sentrin-specific protease 6 is an enzyme that in humans is encoded by the SENP6 gene.

Sentrin-specific protease 2 is an enzyme that in humans is encoded by the SENP2 gene.

ETS-related transcription factor Elf-4 is a protein that in humans is encoded by the ELF4 gene.

Origin recognition complex subunit 1 is a protein that in humans is encoded by the ORC1 gene. It is closely related to CDC6, and both are the same protein in archaea.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000184900 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020265 - 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.
↑ Lapenta V, Chiurazzi P, van der Spek P, Pizzuti A, Hanaoka F, Brahe C (March 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.
1 2 "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)".
↑ Lee J, Lee Y, Lee MJ, Park E, Kang SH, Chung CH, Lee KH, Kim K (October 2008). "Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex". Molecular and Cellular Biology. 28 (19): 6056–65. doi:10.1128/MCB.00583-08. PMC 2546997 . PMID 18644859.
↑ Hardeland U, Steinacher R, Jiricny J, Schär P (March 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.

Maruyama K, Sugano S (January 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, Suyama A, Sugano S (October 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 (March 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.
Tatham MH, Jaffray E, Vaughan OA, Desterro JM, Botting CH, Naismith JH, Hay RT (September 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.
Lin J, Johannsen E, Robertson E, Kieff E (January 2002). "Epstein-Barr virus nuclear antigen 3C putative repression domain mediates coactivation of the LMP1 promoter with EBNA-2". Journal of Virology. 76 (1): 232–42. doi:10.1128/JVI.76.1.232-242.2002. PMC 135708 . PMID 11739688.
Kadoya T, Yamamoto H, Suzuki T, Yukita A, Fukui A, Michiue T, Asahara T, Tanaka K, Asashima M, Kikuchi A (June 2002). "Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of beta-catenin". Molecular and Cellular Biology. 22 (11): 3803–19. doi:10.1128/MCB.22.11.3803-3819.2002. PMC 133821 . PMID 11997515.
Su HL, Li SS (August 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.
Subramanian L, Benson MD, Iñiguez-Lluhí JA (March 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". The Journal of Biological Chemistry. 278 (11): 9134–41. doi: 10.1074/jbc.M210440200 . PMID 12511558.
Eaton EM, Sealy L (August 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 (August 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 (December 2003). "SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression". Genes & Development. 17 (24): 3048–61. doi:10.1101/gad.1153003. PMC 305257 . PMID 14701874.
Reverter D, Lima CD (August 2004). "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 (December 2004). "Distinct in vivo dynamics of vertebrate SUMO paralogues". Molecular Biology of the Cell. 15 (12): 5208–18. doi:10.1091/mbc.E04-07-0589. PMC 532004 . PMID 15456902.
Xu Z, Au SW (March 2005). "Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1". The Biochemical Journal. 386 (Pt 2): 325–30. doi:10.1042/BJ20041210. PMC 1134797 . PMID 15487983.
Ding H, Xu Y, Chen Q, Dai H, Tang Y, Wu J, Shi Y (March 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, Andermarcher E, Hipskind R, Rodriguez M, Schmidt D, Muller S, Jariel-Encontre I, Piechaczyk M (August 2005). "Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation". Molecular and Cellular Biology. 25 (16): 6964–79. doi:10.1128/MCB.25.16.6964-6979.2005. PMC 1190241 . PMID 16055710.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000184900 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020265 - 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.

[pmid9119407-5] Lapenta V, Chiurazzi P, van der Spek P, Pizzuti A, Hanaoka F, Brahe C (March 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.

[entrez-6] 1 2 "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)".

[pmid18644859-7] Lee J, Lee Y, Lee MJ, Park E, Kang SH, Chung CH, Lee KH, Kim K (October 2008). "Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex". Molecular and Cellular Biology. 28 (19): 6056–65. doi:10.1128/MCB.00583-08. PMC 2546997 . PMID 18644859.

[pmid11889051-8] Hardeland U, Steinacher R, Jiricny J, Schär P (March 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.

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SUMO3

Contents

Function

Interactions

Related Research Articles

References

Further reading