DUSP22
entrez
56940
canonical
uniprot
Q9NRW4
canonical
ensembl
ENSG00000112679
resolver
ensp
ENSP00000345281
resolver
ensp
ENSP00000397459
resolver
genesymbol
DUSP22
resolver
genesymbol_syn
JSP1
resolver
genesymbol_syn
LMWDSP2
resolver
genesymbol_syn
MKPX
resolver
hgnc
HGNC:16077
resolver
uniprot
B4DK56
resolver
uniprot
Q59GW2
resolver
uniprot
Q5VWR2
resolver
uniprot
Q96AR1
resolver
uniprot_entry
DUS22_HUMAN
resolver
uniprot_sec
B4DK56
resolver
uniprot_sec
Q59GW2
resolver
uniprot_sec
Q5VWR2
resolver
uniprot_sec
Q96AR1
resolver
amino_acid_sequence
MGNGMNKILPGLYIGNFKDARDAEQLSKNKVTHILSVHDSARPMLEGVKYLCIPAADSPSQNLTRHFKESIKFIHECRLRGESCLVHCLAGVSRSVTLVIAYIMTVTDFGWEDALHTVRAGRSCANPNVGFQRQLQEFEKHEVHQYRQWLKEEYGESPLQDAEEAKNILAAPGILKFWAFLRRL
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
FUNCTION: Dual specificity phosphatase; can dephosphorylate both phosphotyrosine and phosphoserine or phosphothreonine residues (PubMed:24714587, PubMed:38225265). Activates the JNK signaling pathway (PubMed:11717427). Inhibits T-cell receptor signaling and T-cell mediated immune responses, acting, at least in part, by inducing degradation of E3 ubiquitin ligase UBR2 (PubMed:24714587, PubMed:38225265). Dephosphorylates and thereby induces 'Lys-48'-linked ubiquitination of UBR2, leading to proteasomal degradation of UBR2 (PubMed:38225265). Dephosphorylates and thereby inactivates tyrosine kinase LCK (PubMed:24714587). Inhibits UBR2-mediated 'Lys-63'-linked ubiquitination of LCK (PubMed:38225265). May play a role in B-cell receptor (BCR) signaling and B-cell function (By similarity). {ECO:0000250|UniProtKB:Q99N11, ECO:0000269|PubMed:11717427, ECO:0000269|PubMed:24714587, ECO:0000269|PubMed:38225265}.
uniprot
proteins
mass_dalton
20910
uniprot
proteins
mutagenesis
MUTAGEN 57; /note="D->A,N: Over 40-fold decrease in catalytic efficiency for p-nitrophenyl phosphate."; /evidence="ECO:0000269|PubMed:33053837"; MUTAGEN 88; /note="C->S: Does not dephosphorylate UBR2."; /evidence="ECO:0000269|PubMed:38225265"; MUTAGEN 93; /note="S->A,N: Over 150-fold decrease in catalytic efficiency for p-nitrophenyl phosphate."; /evidence="ECO:0000269|PubMed:33053837"; MUTAGEN 128; /note="N->A,D: Over 100-fold decrease in catalytic efficiency for p-nitrophenyl phosphate."; /evidence="ECO:0000269|PubMed:33053837
uniprot
proteins
post_translational_modification
PTM: Myristoylation regulates subcellular location, and is necessary for activation of JNK. {ECO:0000269|PubMed:20553486}.
uniprot
proteins
protein_family
Non-receptor class dual specificity subfamily
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
11717427
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17068812
uniprot
proteins
pubmed
20553486
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24714587
uniprot
proteins
pubmed
25664796
uniprot
proteins
pubmed
33053837
uniprot
proteins
pubmed
38225265
uniprot
proteins
sequence_length
184
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20553486}.
uniprot
proteins