The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9 (Q95815063)

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30 May 2020

title

The Mdm-2 amino terminus is required for Mdm2 binding and SUMO-1 conjugation by the E2 SUMO-1 conjugating enzyme Ubc9 (English)

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30 May 2020

4

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30 May 2020

author name string

T Buschmann

series ordinal

1

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30 May 2020

D Lerner

series ordinal

2

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30 May 2020

C G Lee

series ordinal

3

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30 May 2020

language of work or name

English

0 references

publication date

30 May 2001

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Journal of Biological Chemistry

30 May 2020

published in

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30 May 2020

volume

276

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30 May 2020

page(s)

40389-40395

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30 May 2020

issue

44

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30 May 2020

1 reference

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Felix Hoppe-Seyler Lecture 2000. The ubiquitin system and the N-end rule pathway

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Evolution and function of ubiquitin-like protein-conjugation systems

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Ubiquitin-like proteins: new wines in new bottles

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Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins

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Ubch9 conjugates SUMO but not ubiquitin

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The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme

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In vitro SUMO-1 modification requires two enzymatic steps, E1 and E2

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The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1).

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Conformational flexibility of a ubiquitin conjugation enzyme (E2)

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A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

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SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation

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Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.

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SUMO-1 modification activates the transcriptional response of p53

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SUMO-1 modification of Mdm2 prevents its self-ubiquitination and increases Mdm2 ability to ubiquitinate p53.

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Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2.

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RanBP2 associates with Ubc9p and a modified form of RanGAP1

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Preferential modification of nuclear proteins by a novel ubiquitin-like molecule

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The nuclear dot protein sp100, characterization of domains necessary for dimerization, subcellular localization, and modification by small ubiquitin-like modifiers

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Modulation of ETS-1 transcriptional activity by huUBC9, a ubiquitin-conjugating enzyme

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Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif

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Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system

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SUMO-1 conjugation to human DNA topoisomerase II isozymes

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SUMO-1 conjugation to topoisomerase I: A possible repair response to topoisomerase-mediated DNA damage

21 January 2018

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Covalent modification of the transcriptional repressor tramtrack by the ubiquitin-related protein Smt3 in Drosophila flies

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Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast

21 January 2018

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Interaction of Fas(Apo-1/CD95) with proteins implicated in the ubiquitination pathway

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Covalent modification of the Werner's syndrome gene product with the ubiquitin-related protein, SUMO-1

21 January 2018

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Association of activating transcription factor 2 (ATF2) with the ubiquitin-conjugating enzyme hUBC9. Implication of the ubiquitin/proteasome pathway in regulation of ATF2 in T cells

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Interaction of the Ubc9 human homologue with c-Jun and with the glucocorticoid receptor

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Poly(ADP-ribose) polymerase interacts with a novel human ubiquitin conjugating enzyme: hUbc9

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Mdm2 promotes the rapid degradation of p53

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Regulation of p53 stability by Mdm2

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Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

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JNK targets p53 ubiquitination and degradation in nonstressed cells

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Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53

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Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53.

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Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain

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The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification

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Identifiers

DOI

10.1074/JBC.M103786200

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11384992%20AND%20SRC:MED&resulttype=core&format=json

30 May 2020

1 reference