|Institutional Source||Beutler Lab|
|Gene Name||dual specificity phosphatase 19|
|Synonyms||SKRP1, TS-DSP1, 5930436K22Rik, C79103|
|Is this an essential gene?||Probably non essential (E-score: 0.223)|
|Stock #||R7693 (G1)|
|Chromosomal Location||80617045-80632361 bp(+) (GRCm38)|
|Type of Mutation||missense|
|DNA Base Change (assembly)||A to G at 80617561 bp|
|Amino Acid Change||Threonine to Alanine at position 60 (T60A)|
|Ref Sequence||ENSEMBL: ENSMUSP00000028384 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000028384]|
|Predicted Effect||probably benign
AA Change: T60A
PolyPhen 2 Score 0.001 (Sensitivity: 0.99; Specificity: 0.15)
AA Change: T60A
|Coding Region Coverage||
|MGI Phenotype||FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] 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]|
|Allele List at MGI|
|Other mutations in this stock||
|Other mutations in Dusp19||
(F):5'- CGCTCATGTAATGCACTCCC -3'
(R):5'- GGCAGACACGTCCCTATTTTG -3'
(F):5'- GCTCATGTAATGCACTCCCTGAAC -3'
(R):5'- AGACACGTCCCTATTTTGTTCCTAAC -3'