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Paper Details

Phosphorylation of the proline-rich domain of Xp95 modulates Xp95 interaction with partner proteins.
Biochem J
16
2007
ALG-2 (apoptosis-linked-gene-2 product)-interacting protein X, AMSH, Alix, Bro1 domain, C, CIN85, G2-arrested immature, GST, M-phase cell, M-phase cell lysates, M-phase-arrested mature oocytes, N, PRD, S, SETA, SH3, SH3 domain, SH3-domain kinase-binding protein 1, SH3KBP1, Src homology 3, Thr745, Xenopus, Xenopus orthologue of Alix, Xp95, a-cyano-4-hydroxycinnamate, deubiquitinase, glutathione, glutathione S-transferase, mitotically arrested but, oocyte, oocytes, progesteroneinduced, proline, serum-stimulated mammalian cells, signal transducing adaptor molecule, tumorigenic astrocytes
Amino Acid Sequence, Animals, Calcium-Binding Proteins, Carrier Proteins, Cell Cycle Proteins, Cell Division, Electrophoretic Mobility Shift Assay, Endopeptidases, Endosomal Sorting Complexes Required for Transport, HeLa Cells, Humans, Neoplasm Proteins, Nerve Tissue Proteins, Oocytes, Phosphoproteins, Phosphorylation, Rats, Threonine, Ubiquitin Thiolesterase, Xenopus Proteins, src Homology Domains
Author NameAffiliation
Robert E DejournettThe University of Texas M.D. Anderson Cancer Center
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