Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]
Overall distribution
Tissue specific distribution
Overall distribution
Tissue specific distribution
Gscore (Amp):
0.12
Gscore (Del):
0.00
Recurrently amplified in 1 cancer type(s)
Overall distribution
Tissue specific distribution
Mscore:
0.00
Overall
Tissue specific
Total fusion occurrence:
NA
Overall
Tissue specific
Functional class:
Enzyme
JensenLab PubMed score:
4.50 (Percentile rank: 25.43%)
PubTator score:
4.62 (Percentile rank: 27.43%)
Target development/druggability level:
TdarkThese are targets about which virtually nothing is known. They do not have known drug or small molecule activities that satisfy the activity thresholds detailed below AND satisfy two or more of the following criteria: 1) A PubMed text-mining score from Jensen Lab < 5; 2) <= 3 Gene RIFs; 3) <= 50 Antibodies available according to http://antibodypedia.com.
