SUMO3

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Small ubiquitin-like modifier 3
Protein SUMO3 PDB 1u4a.png
PDB rendering based on 1u4a.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SUMO3 ; SMT3A; SMT3H1; SUMO-3; Smt3B
External IDs OMIM602231 MGI1336201 HomoloGene38251 GeneCards: SUMO3 Gene
RNA expression pattern
PBB GE SUMO3 200740 s at tn.png
PBB GE SUMO3 200739 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6612 20610
Ensembl ENSG00000184900 ENSMUSG00000020265
UniProt P55854 Q9Z172
RefSeq (mRNA) NM_001286416 NM_019929
RefSeq (protein) NP_001273345 NP_064313
Location (UCSC) Chr 17:
73.16 – 73.18 Mb
Chr 10:
77.61 – 77.64 Mb
PubMed search [1] [2]

Small ubiquitin-related modifier 3 is a protein that in humans is encoded by the SUMO3 gene.[1][2]

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][2]

Interactions[edit]

SUMO3 has been shown to interact with ARNTL[3] and Thymine-DNA glycosylase.[4]

References[edit]

  1. ^ Lapenta V, Chiurazzi P, van der Spek P, Pizzuti A, Hanaoka F, Brahe C (Apr 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. 
  2. ^ a b "Entrez Gene: SUMO3 SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)". 
  3. ^ Lee, Jiwon; Lee Yool; Lee Min Joo; Park Eonyoung; Kang Sung Hwan; Chung Chin Ha; Lee Kun Ho; Kim Kyungjin (Oct 2008). "Dual modification of BMAL1 by SUMO2/3 and ubiquitin promotes circadian activation of the CLOCK/BMAL1 complex". Mol. Cell. Biol. (United States) 28 (19): 6056–65. doi:10.1128/MCB.00583-08. PMC 2546997. PMID 18644859. 
  4. ^ Hardeland, Ulrike; Steinacher Roland; Jiricny Josef; Schär Primo (Mar 2002). "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover". EMBO J. (England) 21 (6): 1456–64. doi:10.1093/emboj/21.6.1456. ISSN 0261-4189. PMC 125358. PMID 11889051. 

Further reading[edit]