SUMO3

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SUMO3
Protein SUMO3 PDB 1u4a.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SUMO3, SMT3A, SMT3H1, SUMO-3, Smt3B, small ubiquitin-like modifier 3
External IDs MGI: 1336201 HomoloGene: 38251 GeneCards: SUMO3
RNA expression pattern
PBB GE SUMO3 200740 s at fs.png

PBB GE SUMO3 200739 s at fs.png
More reference expression data
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006936
NM_001286416

NM_001301671
NM_001301672
NM_001301673
NM_019929

RefSeq (protein)

NP_001273345
NP_008867

Location (UCSC) Chr 21: 44.81 – 44.82 Mb Chr 10: 77.61 – 77.64 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Small ubiquitin-related modifier 3 is a protein that in humans is encoded by the SUMO3 gene.[3][4]

Function[edit]

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][4]

Interactions[edit]

SUMO3 has been shown to interact with ARNTL[5] and Thymine-DNA glycosylase.[6]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ 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. 
  4. ^ a b "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)". 
  5. ^ 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 2546997Freely accessible. PMID 18644859. 
  6. ^ 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 125358Freely accessible. PMID 11889051. 

Further reading[edit]