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Article

Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation.

Biochemistry - 26 Aug 2003

Tatham Michael H, Kim Suhkmann, Yu Bin, Jaffray Ellis, Song Jing, Zheng Jian, Rodriguez Manuel S, Hay Ronald T, Chen Yuan

Abstract excerpt

Covalent posttranslational modification of target proteins with ubiquitin and ubiquitin-like proteins regulates many important cellular processes. However, the molecular mechanisms by which these proteins are activated and conjugated to substrates has yet to be fully understood. NMR studies have...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 12924945
DOI: 10.1021/bi0345283

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12924945-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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Role of an N-terminal site of Ubc9 in SUMO-1, -2, and -3 binding and conjugation.PMID 12924945Read ↗

Identification of a substrate recognition site on Ubc9.Semantic proximity Read ↗

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Modification of Ran GTPase-activating protein by the small ubiquitin-related modifier SUMO-1 requires Ubc9, an E2-type ubiquitin-conjugating enzyme homologue.Semantic proximity Read ↗

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