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

SUMO3
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSUMO3, SMT3A, SMT3H1, SUMO-3, Smt3B, small ubiquitin-like modifier 3, small ubiquitin like modifier 3
External IDsOMIM: 602231; MGI: 1336201; HomoloGene: 38251; GeneCards: SUMO3; OMA:SUMO3 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006936
NM_001286416

NM_001301671
NM_001301672
NM_001301673
NM_019929

RefSeq (protein)

NP_001273345
NP_008867

NP_001288600
NP_001288601
NP_001288602
NP_064313

Location (UCSC)Chr 21: 44.81 – 44.82 MbChr 10: 77.44 – 77.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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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

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

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000184900Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020265Ensembl, 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.
  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.
  6. ^ a b "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)".
  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.
  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.

Further reading

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