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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Dual specificity phosphatase 15

VHY, VH1-related member Y, DUSP15
The protein encoded by this gene belongs to the non-receptor class of the protein-tyrosine phosphatase family. The encoded protein has both protein-tyrosine phophatase activity and serine/threonine-specific phosphatase activity, and therefore is known as a dual specificity phosphatase. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MKP-1, ACID, fibrillin-1, DUSP22, DUSP23
Papers on VHY
Virtual Screening with Docking Simulations and Biochemical Evaluation of VHY Phosphatase Inhibitors.
Kim et al., In Chem Pharm Bull (tokyo), 2014
Although VH1-related member Y (VHY) phosphatase is responsible for the pathogenesis of neuroinflammatory diseases, no small-molecule inhibitor of VHY has been reported so far.
Identification of VHY/Dusp15 as a regulator of oligodendrocyte differentiation through a systematic genomics approach.
Hooft van Huijsduijnen et al., Genève, Switzerland. In Plos One, 2011
This effort led to the identification of Dusp15/VHY, a PTP previously believed to be expressed only in testis, as being transcriptionally regulated during OL differentiation and in MS lesions.
Myristoylation of the dual-specificity phosphatase c-JUN N-terminal kinase (JNK) stimulatory phosphatase 1 is necessary for its activation of JNK signaling and apoptosis.
Tonks et al., United States. In Febs J, 2010
JSP1 and its relative DUSP15 are unique among members of the protein tyrosine phosphatase family in that they contain a potential myristoylation site at the N-terminus (MGNGMXK).
Antibody repertoire development in fetal and neonatal piglets. XIII. Hybrid VH genes and the preimmune repertoire revisited.
Wertz et al., Iowa City, United States. In J Immunol, 2006
Two chimeric germline genes (VHZ and VHY), together with VHF and the four genes mentioned above, constitute the major VH genes and these account for > 95% of the preimmune repertoire.
Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase.
Kim et al., Taejŏn, South Korea. In Proteins, 2005
crystal structure of catalytic domain
The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ.
Mustelin et al., Los Angeles, United States. In J Biol Chem, 2004
The smallest active protein-tyrosine phosphatase yet (only 16 kDa) is described here and given the name VHZ for VH1-like member Z because it belongs to the group of small Vaccinia virus VH1-related dual specific phosphatases exemplified by VHR, VHX, and VHY.
VHY, a novel myristoylated testis-restricted dual specificity protein phosphatase related to VHX.
Mustelin et al., Los Angeles, United States. In J Biol Chem, 2004
VHY is a new member of a subgroup of myristoylated VH1-like small dual specificity phosphatases
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