Difference between revisions of "Phosphatase Subfamily STYX"
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=== Function === | === Function === | ||
| − | STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. | + | STYX is catalytically inactive (pseudophosphatase) <cite>Wishart95</cite>. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>. |
| − | STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export <cite>Reiterer13</cite>. | + | |
STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis <cite>Wishart02</cite>. | STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis <cite>Wishart02</cite>. | ||
Revision as of 00:54, 2 October 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily STYX
STYX is a catalytically inactive phosphatase found in most opisthokonts but lost in nematodes.
Evolution
STYX is found in most opisthokonts but lost in nematodes. Although STYX is not found in Drosophila and budding yeast, it is found in other arthropoda and fungi (unpublished data from gOrtholog).
Domain
STYX has a single domain, (inactive) phosphatase domain.
Function
STYX is catalytically inactive (pseudophosphatase) [1]. STYX localizes to the nucleus, competes with DUSP4 for binding to ERK, and acts as a nuclear anchor that regulates ERK nuclear export [2]. STYX also binds to a testicular RNA-binding protein Crhsp-24. This complex is essential for normal spermiogenesis [3].
References
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- Error fetching PMID 11842224:
