|Institutional Source||Beutler Lab|
|Gene Name||dual specificity phosphatase 7|
|Is this an essential gene?||Probably non essential (E-score: 0.207)|
|Stock #||R7856 (G1)|
|Chromosomal Location||106368632-106375724 bp(+) (GRCm38)|
|Type of Mutation||missense|
|DNA Base Change (assembly)||C to A at 106368868 bp|
|Amino Acid Change||Alanine to Glutamic Acid at position 24 (A24E)|
|Ref Sequence||ENSEMBL: ENSMUSP00000126984 (fasta)|
|Gene Model||predicted gene model for transcript(s): [ENSMUST00000172306]|
AA Change: A24E
AA Change: A24E
|Predicted Effect||probably benign
|Coding Region Coverage||
|Validation Efficiency||100% (36/36)|
|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. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795), JNK (see MIM 601158), and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses (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 Dusp7||
(F):5'- TTCTGCAAGGCACAGATGTAG -3'
(R):5'- AATCTAGCAGCAGCAGGGAC -3'
(F):5'- TCAGCCAGAGATCTGCGAG -3'
(R):5'- CTCTTGCAGGGCATGGC -3'