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Showing Protein E3 SUMO-protein ligase ZNF451 (HMDBP14489)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP14489
Secondary Accession Numbers None
Name E3 SUMO-protein ligase ZNF451
Synonyms
  1. Coactivator for steroid receptors
  2. E3 SUMO-protein transferase ZNF451
  3. Zinc finger protein 451
Gene Name ZNF451
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins (PubMed:26524493, PubMed:26524494). Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation (By similarity). Has no activity with SUMO1 (PubMed:26524493). Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11' (PubMed:26524493). Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9' (PubMed:24324267). Plays a role in regulating the transcription of AR targets (PubMed:18656483).
Pathways
  • protein sumoylation
Reactions Not Available
GO Classification
Biological Process
regulation of gene expression
positive regulation of transcription from RNA polymerase II promoter
negative regulation of transforming growth factor beta receptor signaling pathway
protein sumoylation
negative regulation of histone H3-K9 acetylation
negative regulation of transcription initiation from RNA polymerase II promoter
Cellular Component
nucleus
PML body
Molecular Function
metal ion binding
transcription corepressor activity
SUMO ligase activity
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 1061
Molecular Weight 121483.51
Theoretical pI 6.768
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID Q9Y4E5
UniProtKB/Swiss-Prot Entry Name ZN451_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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  7. Hendriks IA, Lyon D, Young C, Jensen LJ, Vertegaal AC, Nielsen ML: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. Nat Struct Mol Biol. 2017 Mar;24(3):325-336. doi: 10.1038/nsmb.3366. Epub 2017 Jan 23. [PubMed:28112733 ]
  8. Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC: Uncovering global SUMOylation signaling networks in a site-specific manner. Nat Struct Mol Biol. 2014 Oct;21(10):927-36. doi: 10.1038/nsmb.2890. Epub 2014 Sep 14. [PubMed:25218447 ]
  9. Hendriks IA, Treffers LW, Verlaan-de Vries M, Olsen JV, Vertegaal ACO: SUMO-2 Orchestrates Chromatin Modifiers in Response to DNA Damage. Cell Rep. 2015 Mar 17;10(10):1778-1791. doi: 10.1016/j.celrep.2015.02.033. Epub 2015 Mar 12. [PubMed:25772364 ]
  10. Xiao Z, Chang JG, Hendriks IA, Sigurethsson JO, Olsen JV, Vertegaal AC: System-wide Analysis of SUMOylation Dynamics in Response to Replication Stress Reveals Novel Small Ubiquitin-like Modified Target Proteins and Acceptor Lysines Relevant for Genome Stability. Mol Cell Proteomics. 2015 May;14(5):1419-34. doi: 10.1074/mcp.O114.044792. Epub 2015 Mar 9. [PubMed:25755297 ]
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  14. Karvonen U, Jaaskelainen T, Rytinki M, Kaikkonen S, Palvimo JJ: ZNF451 is a novel PML body- and SUMO-associated transcriptional coregulator. J Mol Biol. 2008 Oct 10;382(3):585-600. doi: 10.1016/j.jmb.2008.07.016. Epub 2008 Jul 16. [PubMed:18656483 ]
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  16. Cappadocia L, Pichler A, Lima CD: Structural basis for catalytic activation by the human ZNF451 SUMO E3 ligase. Nat Struct Mol Biol. 2015 Dec;22(12):968-75. doi: 10.1038/nsmb.3116. Epub 2015 Nov 2. [PubMed:26524494 ]