PMID- 23404503
OWN - NLM
STAT- MEDLINE
DCOM- 20130530
LR  - 20211021
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 288
IP  - 13
DP  - 2013 Mar 29
TI  - UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase 
      for zinc finger protein 131.
PG  - 9102-11
LID - 10.1074/jbc.M112.438234 [doi]
AB  - Small ubiquitin-like modifier (SUMO), a member of the ubiquitin-related protein 
      family, is covalently conjugated to lysine residues of its substrates in a 
      process referred to as SUMOylation. SUMOylation occurs through a series of 
      enzymatic reactions analogous to that of the ubiquitination pathway, resulting in 
      modification of the biochemical and functional properties of substrates. To date, 
      four mammalian SUMO isoforms, a single heterodimeric SUMO-activating E1 enzyme 
      SAE1/SAE2, a single SUMO-conjugating E2 enzyme ubiquitin-conjugating enzyme E2I 
      (UBC9), and a few subgroups of SUMO E3 ligases have been identified. Several SUMO 
      E3 ligases such as topoisomerase I binding, arginine/serine-rich (TOPORS), TNF 
      receptor-associated factor 7 (TRAF7), and tripartite motif containing 27 (TRIM27) 
      have dual functions as ubiquitin E3 ligases. Here, we demonstrate that the 
      ubiquitin E3 ligase UHRF2 also acts as a SUMO E3 ligase. UHRF2 effectively 
      enhances zinc finger protein 131 (ZNF131) SUMOylation but does not enhance ZNF131 
      ubiquitination. In addition, the SUMO E3 activity of UHRF2 on ZNF131 depends on 
      the presence of SET and RING finger-associated and nuclear localization 
      signal-containing region domains, whereas the critical ubiquitin E3 activity RING 
      domain is dispensable. Our findings suggest that UHRF2 has independent functional 
      domains and regulatory mechanisms for these two distinct enzymatic activities.
FAU - Oh, Yohan
AU  - Oh Y
AD  - Department of Systems Biology, College of Life Science and Biotechnology, Yonsei 
      University, Seoul 120-749, Korea.
FAU - Chung, Kwang Chul
AU  - Chung KC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130212
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Leupeptins)
RN  - 0 (Transcription Factors)
RN  - 0 (Ubiquitin)
RN  - 0 (ZNF131 protein, human)
RN  - 9007-49-2 (DNA)
RN  - EC 2.3.2.27 (UHRF2 protein, human)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
RN  - RF1P63GW3K (benzyloxycarbonylleucyl-leucyl-leucine aldehyde)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Cell Nucleus/metabolism
MH  - Chlorocebus aethiops
MH  - DNA/metabolism
MH  - DNA-Binding Proteins/*metabolism
MH  - Dimerization
MH  - HEK293 Cells
MH  - Humans
MH  - Leupeptins/pharmacology
MH  - Models, Biological
MH  - Proteasome Endopeptidase Complex/metabolism
MH  - Protein Binding
MH  - Protein Processing, Post-Translational
MH  - Protein Structure, Tertiary
MH  - RNA Interference
MH  - Transcription Factors/*metabolism
MH  - Ubiquitin/chemistry/metabolism
MH  - Ubiquitin-Protein Ligases/metabolism/*physiology
PMC - PMC3610983
EDAT- 2013/02/14 06:00
MHDA- 2013/06/01 06:00
PMCR- 2014/03/29
CRDT- 2013/02/14 06:00
PHST- 2013/02/14 06:00 [entrez]
PHST- 2013/02/14 06:00 [pubmed]
PHST- 2013/06/01 06:00 [medline]
PHST- 2014/03/29 00:00 [pmc-release]
AID - S0021-9258(19)35071-9 [pii]
AID - M112.438234 [pii]
AID - 10.1074/jbc.M112.438234 [doi]
PST - ppublish
SO  - J Biol Chem. 2013 Mar 29;288(13):9102-11. doi: 10.1074/jbc.M112.438234. Epub 2013 
      Feb 12.