SIAH-1 interacts with mammalian polyhomeotic homologues HPH2 and affects its stability via the ubiquitin-proteasome pathway

Biochemical and Biophysical Research Communications

Volumn 397, Issue 3, 2010, Pages 391-396

  Wu, Huiling ^a   Lin, Ying ^a   Shi, Yan ^a   Qian, Wei ^a   Tian, Zhipeng ^a   Yu, Yao ^b   Huo, Keke ^a  

^a FUDAN UNIVERSITY   (China)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

Degradation; HPH2; SIAH 1; Ubiquitination

Indexed keywords

CYSTEINE; PROTEASOME; PROTEIN; PROTEIN HPH 2; PROTEIN SIAH 1; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; FEMALE; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; MAMMAL; MOLECULAR DYNAMICS; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; REGULATORY MECHANISM; UBIQUITINATION;

CELL LINE; HELA CELLS; HUMANS; NUCLEAR PROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN STABILITY; TRANSCRIPTION FACTORS; TWO-HYBRID SYSTEM TECHNIQUES; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES; UBIQUITINATION;

HOMO SAPIENS; MAMMALIA;

EID: 77954218833     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.05.024     Document Type: Article

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