BAIT

STUB1

0610033N24Rik, 2210017D18Rik, 2310040B03Rik, AW046544, Chip
STIP1 homology and U-Box containing protein 1
GO Process (15)
GO Function (16)
GO Component (9)
Mus musculus
PREY

UBE2N

HEL-S-71, UBC13, UBCHBEN; UBC13, UbcH-ben, UbcH13
ubiquitin-conjugating enzyme E2N
GO Process (30)
GO Function (7)
GO Component (8)
Homo sapiens

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.

Zhang M, Windheim M, Roe SM, Peggie M, Cohen P, Prodromou C, Pearl LH

CHIP is a dimeric U box E3 ubiquitin ligase that binds Hsp90 and/or Hsp70 via its TPR-domain, facilitating ubiquitylation of chaperone bound client proteins. We have determined the crystal structure of CHIP bound to an Hsp90 C-terminal decapeptide. The structure explains how CHIP associates with either chaperone type and reveals an unusual asymmetric homodimer in which the protomers adopt radically ... [more]

Mol. Cell Nov. 23, 2005; 20(4);525-38 [Pubmed: 16307917]

Throughput

  • Low Throughput

Curated By

  • BioGRID