For the Mouse gene set with the same name, see BIOCARTA_STATHMIN_PATHWAY

Systematic name M16966
Brief description Stathmin and breast cancer resistance to antimicrotubule agents
Full description or abstract Stathmin is a ubiquitous, cytosolic 19-kDa protein, which is phosphorylated on up to four sites in response to many regulatory signals within cells. Its molecular characterization indicates a functional organization including an N-terminal regulatory domain that bears the phosphorylation sites, linked to a putative alpha-helical binding domain predicted to participate in coiled-coil, protein-protein interactions. In addtion to the protein kinases that phospjhorylate Stathmin such as CaMK, MAPK, p34cdc2, PKA, a few other proteins have been suggested to interact with stathmin in vivo. One of them was identified as BiP, a member of the hsp70 heat-shock protein family. Another is a previously unidentified, putative serine/threonine kinase, KIS, which might be regulated by stathmin or, more likely, be part of the kinases controlling its phosphorylation state. Finally, two proteins, CC1 and CC2, predicted to form alpha-helices participating in coiled-coil interacting structures. It has been also suggest that the action of antimicrotubule drugs can be affected by stathmin in at least two ways: (a) altered drug binding; and (b) growth arrest at the G2 to M boundary. Mutant p53 breast cancers exhibiting high levels of stathmin may be resistant to antimicrotubule agents.
Collection C2: Curated
      CP: Canonical Pathways
            CP:BIOCARTA: BioCarta Pathways
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Source species Homo sapiens
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Version history 7.0: Changed members. Upgraded to final version of Biocarta.

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