NOP53
entrez
29997
canonical
uniprot
Q9NZM5
canonical
ensembl
ENSG00000105373
resolver
ensp
ENSP00000246802
resolver
enst
ENST00000246802
resolver
genesymbol
NOP53
resolver
genesymbol_syn
GLT
resolver
genesymbol_syn
GLTSCR2
resolver
genesymbol_syn
PICT1
resolver
hgnc
HGNC:4333
resolver
uniprot
Q9BTC6
resolver
uniprot
Q9HAX6
resolver
uniprot
Q9NPP1
resolver
uniprot
Q9NPR4
resolver
uniprot
Q9UFI2
resolver
uniprot_entry
NOP53_HUMAN
resolver
uniprot_sec
Q9BTC6
resolver
uniprot_sec
Q9HAX6
resolver
uniprot_sec
Q9NPP1
resolver
uniprot_sec
Q9NPR4
resolver
uniprot_sec
Q9UFI2
resolver
amino_acid_sequence
MAAGGSGVGGKRSSKSDADSGFLGLRPTSVDPALRRRRRGPRNKKRGWRRLAQEPLGLEVDQFLEDVRLQERTSGGLLSEAPNEKLFFVDTGSKEKGLTKKRTKVQKKSLLLKKPLRVDLILENTSKVPAPKDVLAHQVPNAKKLRRKEQLWEKLAKQGELPREVRRAQARLLNPSATRAKPGPQDTVERPFYDLWASDNPLDRPLVGQDEFFLEQTKKKGVKRPARLHTKPSQAPAVEVAPAGASYNPSFEDHQTLLSAAHEVELQRQKEAEKLERQLALPATEQAATQESTFQELCEGLLEESDGEGEPGQGEGPEAGDAEVCPTPARLATTEKKTEQQRRREKAVHRLRVQQAALRAARLRHQELFRLRGIKAQVALRLAELARRQRRRQARREAEADKPRRLGRLKYQAPDIDVQLSSELTDSLRTLKPEGNILRDRFKSFQRRNMIEPRERAKFKRKYKVKLVEKRAFREIQL
uniprot
proteins
function
FUNCTION: Nucleolar protein which is involved in the integration of the 5S RNP into the ribosomal large subunit during ribosome biogenesis (PubMed:24120868). In ribosome biogenesis, may also play a role in rRNA transcription (PubMed:27729611). Also functions as a nucleolar sensor that regulates the activation of p53/TP53 in response to ribosome biogenesis perturbation, DNA damage and other stress conditions (PubMed:21741933, PubMed:24120868, PubMed:27829214). DNA damage or perturbation of ribosome biogenesis disrupt the interaction between NOP53 and RPL11 allowing RPL11 transport to the nucleoplasm where it can inhibit MDM2 and allow p53/TP53 activation (PubMed:24120868, PubMed:27829214). It may also positively regulate the function of p53/TP53 in cell cycle arrest and apoptosis through direct interaction, preventing its MDM2-dependent ubiquitin-mediated proteasomal degradation (PubMed:22522597). Originally identified as a tumor suppressor, it may also play a role in cell proliferation and apoptosis by positively regulating the stability of PTEN, thereby antagonizing the PI3K-AKT/PKB signaling pathway (PubMed:15355975, PubMed:16971513, PubMed:27729611). May also inhibit cell proliferation and increase apoptosis through its interaction with NF2 (PubMed:21167305). May negatively regulate NPM1 by regulating its nucleoplasmic localization, oligomerization and ubiquitin-mediated proteasomal degradation (PubMed:25818168). Thereby, may prevent NPM1 interaction with MYC and negatively regulate transcription mediated by the MYC-NPM1 complex (PubMed:25956029). May also regulate cellular aerobic respiration (PubMed:24556985). In the cellular response to viral infection, may play a role in the attenuation of interferon-beta through the inhibition of RIGI (PubMed:27824081). {ECO:0000269|PubMed:15355975, ECO:0000269|PubMed:16971513, ECO:0000269|PubMed:21167305, ECO:0000269|PubMed:21741933, ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24120868, ECO:0000269|PubMed:24556985, ECO:0000269|PubMed:25818168, ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:27729611, ECO:0000269|PubMed:27824081, ECO:0000269|PubMed:27829214}.
uniprot
proteins
mass_dalton
54389
uniprot
proteins
mutagenesis
MUTAGEN 233; /note="S->A: Decreased phosphorylation, degradation and increased interaction with RPL11 in response to DNA damage; when associated with A-289."; /evidence="ECO:0000269|PubMed:27829214"; MUTAGEN 233; /note="S->D: Loss of localization to the nucleolus and in response to DNA damage increased degradation and decreased interaction with RPL11; when associated with D-289."; /evidence="ECO:0000269|PubMed:27829214"; MUTAGEN 289; /note="T->A: Decreased degradation in response to DNA damage. Decreased phosphorylation, degradation and increased interaction with RPL11 in response to DNA damage; when associated with A-233."; /evidence="ECO:0000269|PubMed:27829214"; MUTAGEN 289; /note="T->D: Loss of localization to the nucleolus and in response to DNA damage increased degradation and decreased interaction with RPL11; when associated with D-233."; /evidence="ECO:0000269|PubMed:27829214
uniprot
proteins
post_translational_modification
PTM: Ubiquitin-mediated proteasomal degradation is regulated by c-JUN. It is associated with relocalization to the nucleoplasm and decreased homooligomerization. {ECO:0000269|PubMed:26903295}.; PTM: Phosphorylated upon DNA damage probably by ATM and DNA-PK; may regulate NOP53 degradation. {ECO:0000269|PubMed:27829214}.
uniprot
proteins
protein_family
NOP53 family
uniprot
proteins
pubmed
10196275
uniprot
proteins
pubmed
10708517
uniprot
proteins
pubmed
12429849
uniprot
proteins
pubmed
15355975
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16971513
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20042497
uniprot
proteins
pubmed
21167305
uniprot
proteins
pubmed
21741933
uniprot
proteins
pubmed
22292050
uniprot
proteins
pubmed
22522597
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24120868
uniprot
proteins
pubmed
24556985
uniprot
proteins
pubmed
24735870
uniprot
proteins
pubmed
24923447
uniprot
proteins
pubmed
25818168
uniprot
proteins
pubmed
25956029
uniprot
proteins
pubmed
26903295
uniprot
proteins
pubmed
27323397
uniprot
proteins
pubmed
27729611
uniprot
proteins
pubmed
27824081
uniprot
proteins
pubmed
27829214
uniprot
proteins
sequence_length
478
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:10196275, ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:20042497, ECO:0000269|PubMed:22292050, ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24923447, ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:27729611, ECO:0000269|PubMed:27829214}. Nucleus, nucleoplasm {ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24923447, ECO:0000269|PubMed:26903295, ECO:0000269|PubMed:27323397}. Note=In the nucleolus may be more specifically localized to the fibrillar center (PubMed:27729611). Mainly nucleolar it relocalizes to the nucleoplasm under specific conditions including ribosomal stress enabling it to interact and regulate nucleoplasmic proteins like p53/TP53 (PubMed:22522597, PubMed:24923447, PubMed:26903295, PubMed:27323397). Also detected in the cytosol (PubMed:24923447, PubMed:27824081). {ECO:0000269|PubMed:22522597, ECO:0000269|PubMed:24923447, ECO:0000269|PubMed:26903295, ECO:0000269|PubMed:27323397, ECO:0000269|PubMed:27729611, ECO:0000269|PubMed:27824081}.
uniprot
proteins