DRG1
entrez
4733
canonical
uniprot
Q9Y295
canonical
ensembl
ENSG00000185721
resolver
ensp
ENSP00000329715
resolver
enst
ENST00000331457
resolver
genesymbol
DRG1
resolver
genesymbol_syn
NEDD3
resolver
hgnc
HGNC:3029
resolver
uniprot
B2RDS8
resolver
uniprot
Q6FGP8
resolver
uniprot
Q8WW69
resolver
uniprot
Q9UGF2
resolver
uniprot_entry
DRG1_HUMAN
resolver
uniprot_sec
B2RDS8
resolver
uniprot_sec
Q6FGP8
resolver
uniprot_sec
Q8WW69
resolver
uniprot_sec
Q9UGF2
resolver
activity_regulation
ACTIVITY REGULATION: The GTPase activity is enhanced by potassium ions as well as by DFRP1 binding. {ECO:0000269|PubMed:23711155}.
uniprot
proteins
amino_acid_sequence
MSSTLAKIAEIEAEMARTQKNKATAHHLGLLKARLAKLRRELITPKGGGGGGPGEGFDVAKTGDARIGFVGFPSVGKSTLLSNLAGVYSEVAAYEFTTLTTVPGVIRYKGAKIQLLDLPGIIEGAKDGKGRGRQVIAVARTCNLILIVLDVLKPLGHKKIIENELEGFGIRLNSKPPNIGFKKKDKGGINLTATCPQSELDAETVKSILAEYKIHNADVTLRSDATADDLIDVVEGNRVYIPCIYVLNKIDQISIEELDIIYKVPHCVPISAHHRWNFDDLLEKIWDYLKLVRIYTKPKGQLPDYTSPVVLPYSRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVGKDHTLEDEDVIQIVKK
uniprot
proteins
disease_involvement
DISEASE: Tan-Almurshedi syndrome (TANALS) [MIM:620641]: An autosomal recessive neurodevelopmental disorder characterized by global developmental delay, intellectual deficit, poor or absent speech, failure to thrive, short stature, microcephaly, and craniofacial anomalies. {ECO:0000269|PubMed:37179472}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of the gamma-phosphate bond in GTP (PubMed:23711155, PubMed:29915238, PubMed:37179472). Appears to have an intrinsic GTPase activity that is stimulated by ZC3H15/DFRP1 binding likely by increasing the affinity for the potassium ions (PubMed:23711155). When hydroxylated at C-3 of 'Lys-22' by JMJD7, may bind to RNA and play a role in translation (PubMed:19819225, PubMed:29915238). Binds to microtubules and promotes microtubule polymerization and stability that are required for mitotic spindle assembly during prophase to anaphase transition. GTPase activity is not necessary for these microtubule-related functions (PubMed:28855639). {ECO:0000269|PubMed:19819225, ECO:0000269|PubMed:23711155, ECO:0000269|PubMed:28855639, ECO:0000269|PubMed:29915238, ECO:0000269|PubMed:37179472}.
uniprot
proteins
mass_dalton
40542
uniprot
proteins
mutagenesis
MUTAGEN 22; /note="K->A: Impairs JMJD7-mediated hydroxylation."; /evidence="ECO:0000269|PubMed:29915238"; MUTAGEN 100; /note="T->D: Reduces the GTPase activity."; /evidence="ECO:0000269|PubMed:23711155"; MUTAGEN 117; /note="D->A: Loss of GTPase activity."; /evidence="ECO:0000269|PubMed:37179472
uniprot
proteins
post_translational_modification
PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli. {ECO:0000269|PubMed:17709345}.; PTM: Phosphorylated at Thr-100 by STK16. {ECO:0000269|PubMed:18184589}.; PTM: Hydroxylated (with S stereochemistry) at C-3 of Lys-22 by JMJD7; this modification hinders trypsin-catalyzed proteolysis in vitro. {ECO:0000269|PubMed:29915238, ECO:0000269|PubMed:35410347}.; PTM: Polyubiquitinated; this modification induces proteolytic degradation and is impaired by interaction with ZC3H15. {ECO:0000250|UniProtKB:P32233}.
uniprot
proteins
protein_family
OBG GTPase family
uniprot
proteins
protein_family
TRAFAC class OBG-HflX-like GTPase superfamily
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
10760581
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15676025
uniprot
proteins
pubmed
17709345
uniprot
proteins
pubmed
18184589
uniprot
proteins
pubmed
19819225
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23711155
uniprot
proteins
pubmed
25944354
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28855639
uniprot
proteins
pubmed
29915238
uniprot
proteins
pubmed
35410347
uniprot
proteins
pubmed
37179472
uniprot
proteins
pubmed
9824680
uniprot
proteins
sequence_length
367
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29915238}. Cytoplasm {ECO:0000269|PubMed:15676025, ECO:0000269|PubMed:19819225, ECO:0000269|PubMed:29915238}. Note=The DRG1-ZC3H15/DFRP1 complex associates with polysomes.
uniprot
proteins