RBP Type
Non-canonical_RBPs
Diseases
SARS-COV-2
Drug
N.A.
Main interacting RNAs
N.A.
Moonlighting functions
Metabolic enzyme
Localizations
N.A.
BulkPerturb-seq
Ensembl ID ENSG00000165609 Gene ID
11164
Accession
8052
Symbol
NUDT5
Alias
YSA1;YSA1H;YSAH1;hNUDT5
Full Name
nudix hydrolase 5
Status
Confidence
Length
30815 bases
Strand
Minus strand
Position
10 : 12165330 - 12196144
RNA binding domain
N.A.
Summary
This gene belongs to the Nudix (nucleoside diphosphate linked moiety X) hydrolase superfamily. The encoded enzyme catalyzes the hydrolysis of modified nucleoside diphosphates, including ADP-ribose (ADPR) and 8-oxoGua-containing 8-oxo-dADP and 8-oxo-dGDP. Protein-bound ADP ribose can be hazardous to the cell because it can modify some amino acid residues, resulting in the inhibition of ATP-activated potassium channels. 8-oxoGua is an oxidized form of guanine that can potentially alter genetic information by pairing with adenine and cytosine in RNA. Presence of 8-oxoGua in RNA results in formation of abnormal proteins due to translational errors. [provided by RefSeq, Aug 2013]
RNA binding domains (RBDs)
Protein
Domain
Pfam ID
E-value
Domain number
RNA binding proteomes (RBPomes)
Pubmed ID
Full Name
Cell
Author
Time
Doi
Literatures on RNA binding capacity
Pubmed ID
Title
Author
Time
Journal
Name
Transcript ID
bp
Protein
Translation ID
NUDT5-207
ENST00000491614
3195
219aa
ENSP00000419628
NUDT5-202
ENST00000378937
919
232aa
ENSP00000368219
NUDT5-204
ENST00000378952
917
No protein
-
NUDT5-206
ENST00000476462
622
137aa
ENSP00000436844
NUDT5-203
ENST00000378940
1126
186aa
ENSP00000368222
NUDT5-201
ENST00000378927
1258
180aa
ENSP00000368209
NUDT5-208
ENST00000498825
473
No protein
-
NUDT5-205
ENST00000444732
410
97aa
ENSP00000407856
Pathway ID
Pathway Name
Source
ensgID
Trait
pValue
Pubmed ID
ensgID SNP Chromosome Position
Trait PubmedID Or or BEAT
EFO ID
Protein-Protein Interaction (PPI)
Ensembl ID
Source
Target
Species
Protein ID
Perc_pos
Perc_id
Species
Protein ID
Perc_pos
Perc_id
Ensembl ID
Source
Target
Species
Protein ID
Perc_pos
Perc_id
Species
Protein ID
Perc_pos
Perc_id
Go ID
Go term
No. evidence
Entries
Species
Category
GO:0000287 enables magnesium ion binding 1 IDA Homo_sapiens(9606) Function GO:0005515 enables protein binding 1 IPI Homo_sapiens(9606) Function GO:0005634 located_in nucleus 3 HDA,IBA,IDA Homo_sapiens(9606) Component GO:0005829 located_in cytosol 1 TAS Homo_sapiens(9606) Component GO:0006338 involved_in chromatin remodeling 1 IDA Homo_sapiens(9606) Process GO:0006753 involved_in nucleoside phosphate metabolic process 1 IBA Homo_sapiens(9606) Process GO:0009117 involved_in nucleotide metabolic process 1 NAS Homo_sapiens(9606) Process GO:0009191 involved_in ribonucleoside diphosphate catabolic process 1 IDA Homo_sapiens(9606) Process GO:0016779 enables nucleotidyltransferase activity 1 IDA Homo_sapiens(9606) Function GO:0019144 enables ADP-sugar diphosphatase activity 1 IDA Homo_sapiens(9606) Function GO:0019303 involved_in D-ribose catabolic process 2 IDA,NAS Homo_sapiens(9606) Process GO:0019693 involved_in ribose phosphate metabolic process 1 IBA Homo_sapiens(9606) Process GO:0030515 enables snoRNA binding 1 ISS Homo_sapiens(9606) Function GO:0042802 enables identical protein binding 1 IPI Homo_sapiens(9606) Function GO:0042803 enables protein homodimerization activity 1 IDA Homo_sapiens(9606) Function GO:0044715 enables 8-oxo-dGDP phosphatase activity 1 IDA Homo_sapiens(9606) Function GO:0044716 enables 8-oxo-GDP phosphatase activity 1 IEA Homo_sapiens(9606) Function GO:0047631 enables ADP-ribose diphosphatase activity 3 EXP,IBA,IDA Homo_sapiens(9606) Function GO:0055086 involved_in nucleobase-containing small molecule metabolic process 1 TAS Homo_sapiens(9606) Process GO:0070062 located_in extracellular exosome 1 HDA Homo_sapiens(9606) Component GO:0140933 NOT enables 5-(N(7)-methylguanosine 5-triphospho)-[mRNA] hydrolase activity 1 ISS Homo_sapiens(9606) Function GO:1990966 involved_in ATP generation from poly-ADP-D-ribose 1 IDA Homo_sapiens(9606) Process
Copyright © 2023, Bioinformatics Center, Sun Yat-sen Memorial Hospital, Sun Yat-sen University, China. All Rights Reserved.