DNASE2
entrez
1777
canonical
uniprot
O00115
canonical
ensembl
ENSG00000105612
resolver
ensp
ENSP00000222219
resolver
genesymbol
DNASE2
resolver
genesymbol_syn
DNASE2A
resolver
genesymbol_syn
DNL2
resolver
hgnc
HGNC:2960
resolver
uniprot
B2RD06
resolver
uniprot
B7Z4K6
resolver
uniprot
O43910
resolver
uniprot_entry
DNS2A_HUMAN
resolver
uniprot_sec
B2RD06
resolver
uniprot_sec
B7Z4K6
resolver
uniprot_sec
O43910
resolver
amino_acid_sequence
MIPLLLAALLCVPAGALTCYGDSGQPVDWFVVYKLPALRGSGEAAQRGLQYKYLDESSGGWRDGRALINSPEGAVGRSLQPLYRSNTSQLAFLLYNDQPPQPSKAQDSSMRGHTKGVLLLDHDGGFWLVHSVPNFPPPASSAAYSWPHSACTYGQTLLCVSFPFAQFSKMGKQLTYTYPWVYNYQLEGIFAQEFPDLENVVKGHHVSQEPWNSSITLTSQAGAVFQSFAKFSKFGDDLYSGWLAAALGTNLQVQFWHKTVGILPSNCSDIWQVLNVNQIAFPGPAGPSFNSTEDHSKWCVSPKGPWTCVGDMNRNQGEEQRGGGTLCAQLPALWKAFQPLVKNYQPCNGMARKPSRAYKI
uniprot
proteins
disease_involvement
DISEASE: Autoinflammatory-pancytopenia syndrome (AIPCS) [MIM:619858]: An autosomal recessive disorder characterized by severe anemia and thrombocytopenia apparent from early infancy, hepatosplenomegaly, and recurrent fevers associated with a hyperinflammatory state. Additional systemic features may include chronic diarrhea, proteinuria with renal disease, liver fibrosis with elevated liver enzymes, deforming arthropathy, and vasculitic skin lesions. Some patients may have motor delay or learning difficulties associated with subcortical white matter lesions on brain imaging. {ECO:0000269|PubMed:29259162, ECO:0000269|PubMed:31775019}. Note=The disease is caused by variants affecting the gene represented in this entry. The genetic variation producing the missense variant p.G116A, associated with AIPCS, has been shown to predominantly affect splicing, leading to in-frame deletion of exon 4, encoding amino acids 116 to 171. The protein resulting from this aberrant splicing may be unstable. {ECO:0000269|PubMed:29259162}.
uniprot
proteins
ec_number
3.1.22.1
uniprot
proteins
function
FUNCTION: Hydrolyzes DNA under acidic conditions with a preference for double-stranded DNA. Plays a major role in the clearance of nucleic acids generated through apoptosis, hence preventing autoinflammation (PubMed:29259162, PubMed:31775019). Necessary for proper fetal development and for definitive erythropoiesis in fetal liver and bone marrow, where it degrades nuclear DNA expelled from erythroid precursor cells (PubMed:29259162). {ECO:0000269|PubMed:29259162, ECO:0000269|PubMed:31775019}.
uniprot
proteins
mass_dalton
39581
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 86; /note="N->Q: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-212; Q-266 and Q-290."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 151; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 159; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 212; /note="N->Q: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-266 and Q-290."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 266; /note="N->Q: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-212 and Q-290."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 267; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 290; /note="N->Q: Reduced N-glycosylation, complete loss of N-glycosylation; when associated with Q-86; Q-212 and Q-266."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 295; /note="H->A,K,N,R,S: Loss of activity, but not of DNA-binding."; /evidence="ECO:0000269|PubMed:12594037"; MUTAGEN 299; /note="C->A: No effect."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 308; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 327; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12558498"; MUTAGEN 347; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:12558498
uniprot
proteins
post_translational_modification
PTM: Glycosylated. Genetic variations that affect N-glycosylation sites reduce activity, but enzymatic deglycosylation has no effect. {ECO:0000269|PubMed:11906178, ECO:0000269|PubMed:12558498, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218}.
uniprot
proteins
protein_family
DNase II family
uniprot
proteins
pubmed
11906178
uniprot
proteins
pubmed
12558498
uniprot
proteins
pubmed
12594037
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
29259162
uniprot
proteins
pubmed
31775019
uniprot
proteins
pubmed
9446563
uniprot
proteins
pubmed
9647784
uniprot
proteins
pubmed
9714827
uniprot
proteins
pubmed
9812984
uniprot
proteins
pubmed
9924608
uniprot
proteins
sequence_length
360
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P56542}.
uniprot
proteins