DTD1
entrez
92675
canonical
uniprot
Q8TEA8
canonical
ensembl
ENSG00000125821
resolver
ensp
ENSP00000366672
resolver
ensp
ENSP00000495845
resolver
ensp
ENSP00000586848
resolver
enst
ENST00000377452
resolver
enst
ENST00000494921
resolver
enst
ENST00000916789
resolver
genesymbol
DTD1
resolver
genesymbol_syn
C20orf88
resolver
genesymbol_syn
DUEB
resolver
genesymbol_syn
HARS2
resolver
hgnc
HGNC:16219
resolver
uniprot
A0A2R8Y6X2
resolver
uniprot
A8K5X5
resolver
uniprot
D3DW37
resolver
uniprot
Q496D1
resolver
uniprot
Q5W184
resolver
uniprot
Q8WXU8
resolver
uniprot
Q9BW67
resolver
uniprot
Q9H464
resolver
uniprot
Q9H474
resolver
uniprot_entry
A0A2R8Y6X2_HUMAN
resolver
uniprot_entry
DTD1_HUMAN
resolver
uniprot_sec
A8K5X5
resolver
uniprot_sec
D3DW37
resolver
uniprot_sec
Q496D1
resolver
uniprot_sec
Q5W184
resolver
uniprot_sec
Q8WXU8
resolver
uniprot_sec
Q9BW67
resolver
uniprot_sec
Q9H464
resolver
uniprot_sec
Q9H474
resolver
amino_acid_sequence
MKAVVQRVTRASVTVGGEQISAIGRGICVLLGISLEDTQKELEHMVRKILNLRVFEDESGKHWSKSVMDKQYEILCVSQFTLQCVLKGNKPDFHLAMPTEQAEGFYNSFLEQLRKTYRPELIKDGKFGAYMQVHIQNDGPVTIELESPAPGTATSDPKQLSKLEKQQQRKEKTRAKGPSESSKERNTPRKEDRSASSGAEGDVSSEREP
uniprot
proteins
ec_number
3.1.1.96
uniprot
proteins
function
FUNCTION: Possible ATPase (PubMed:15653697) involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes (PubMed:20065034). {ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}.; FUNCTION: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality. {ECO:0000250|UniProtKB:Q8IIS0}.
uniprot
proteins
mass_dalton
23424
uniprot
proteins
post_translational_modification
PTM: Preferentially phosphorylated in cells arrested early in S phase (PubMed:15653697). Phosphorylation in the C-terminus weakens the interaction with CDC45 (PubMed:20065034). {ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}.
uniprot
proteins
protein_family
DTD family
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
12392168
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15653697
uniprot
proteins
pubmed
17264083
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20065034
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
209
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15653697, ECO:0000269|PubMed:20065034}. Cytoplasm {ECO:0000250|UniProtKB:Q8IIS0}. Note=Associated with chromatin at some replication origins containing functional DNA-unwinding elements (PubMed:20065034).
uniprot
proteins