O60356 · NUPR1_HUMAN
- ProteinNuclear protein 1
- GeneNUPR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transcription regulator that converts stress signals into a program of gene expression that empowers cells with resistance to the stress induced by a change in their microenvironment. Thereby participates in regulation of many process namely cell-cycle, apoptosis, autophagy and DNA repair responses (PubMed:11056169, PubMed:11940591, PubMed:16300740, PubMed:16478804, PubMed:18690848, PubMed:19650074, PubMed:19723804, PubMed:20181828, PubMed:22565310, PubMed:22858377, PubMed:30451898).
Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848).
Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (PubMed:22565310).
Negatively regulates apoptosis through interaction with PTMA (PubMed:16478804).
Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828).
Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity).
Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity).
Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (PubMed:19650074).
Coactivator of PAX2 transcription factor activity, both by recruiting EP300 to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (PubMed:11940591).
Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (PubMed:16300740).
Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (PubMed:19723804).
Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity).
Also required for LHB expression and ovarian maturation (By similarity).
Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity).
Controls cell cycle progression and protects cells from genotoxic stress induced by doxorubicin through the complex formation with TP53 and EP300 that binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848).
Protects pancreatic cancer cells from stress-induced cell death by binding the RELB promoter and activating its transcription, leading to IER3 transactivation (PubMed:22565310).
Negatively regulates apoptosis through interaction with PTMA (PubMed:16478804).
Inhibits autophagy-induced apoptosis in cardiac cells through FOXO3 interaction, inducing cytoplasmic translocation of FOXO3 thereby preventing the FOXO3 association with the pro-autophagic BNIP3 promoter (PubMed:20181828).
Inhibits cell growth and facilitates programmed cell death by apoptosis after adriamycin-induced DNA damage through transactivation of TP53 (By similarity).
Regulates methamphetamine-induced apoptosis and autophagy through DDIT3-mediated endoplasmic reticulum stress pathway (By similarity).
Participates in DNA repair following gamma-irradiation by facilitating DNA access of the transcription machinery through interaction with MSL1 leading to inhibition of histone H4' Lys-16' acetylation (H4K16ac) (PubMed:19650074).
Coactivator of PAX2 transcription factor activity, both by recruiting EP300 to increase PAX2 transcription factor activity and by binding PAXIP1 to suppress PAXIP1-induced inhibition on PAX2 (PubMed:11940591).
Positively regulates cell cycle progression through interaction with COPS5 inducing cytoplasmic translocation of CDKN1B leading to the CDKN1B degradation (PubMed:16300740).
Coordinates, through its interaction with EP300, the assiociation of MYOD1, EP300 and DDX5 to the MYOG promoter, leading to inhibition of cell-cycle progression and myogenic differentiation promotion (PubMed:19723804).
Negatively regulates beta cell proliferation via inhibition of cell-cycle regulatory genes expression through the suppression of their promoter activities (By similarity).
Also required for LHB expression and ovarian maturation (By similarity).
Exacerbates CNS inflammation and demyelination upon cuprizone treatment (By similarity).
Miscellaneous
Mediates resistance to anticancer drugs, namely taxol, doxorubicin, gemcitabine.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNuclear protein 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO60356
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 33 | Impairs interaction with RNF2. | ||||
Sequence: A → Q | ||||||
Mutagenesis | 68 | Impairs interaction with RNF2. | ||||
Sequence: T → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 124 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000058007 | 1-82 | UniProt | Nuclear protein 1 | |||
Sequence: MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 58 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated in vitro by PKA and CK. Phosphorylation promotes DNA-binding activity.
Acetylated by EP300 in vitro.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed, with high levels in liver, pancreas, prostate, ovary, colon, thyroid, spinal cord, trachea and adrenal gland, moderate levels in heart, placenta, lung, skeletal muscle, kidney, testis, small intestine, stomach and lymph node, and low levels in brain, spleen, thymus and bone marrow. Not detected in peripheral blood leukocytes.
Induction
Up-regulated by stress agents, such as nutrient deprivation (at protein level) (PubMed:22565310).
Up-regulation by gamma-irradiation is eventually followed by down-regulation (PubMed:19650074).
Expression increases with the tumor aggressiveness. up-regulated by DNA-damaging agent such as doxorubicin (PubMed:18690848).
Up-regulation by gamma-irradiation is eventually followed by down-regulation (PubMed:19650074).
Expression increases with the tumor aggressiveness. up-regulated by DNA-damaging agent such as doxorubicin (PubMed:18690848).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Monomer. Directly interacts with MSL1 and binds MORF4L1, two components of histone acetyltransferase complex; the interaction with MORF4L1 may be mediated by MSL1 (PubMed:19650074).
Interacts with EP300; this interaction enhances the effect of EP300 on PAX2 transcription factor activity (PubMed:11940591).
Interacts with PAXIP1; this interaction prevents PAXIP1 inhibition of PAX2 transcription factor activity (PubMed:11940591).
Interacts with COPS5; this interaction allows COPS5-dependent CDKN1B nuclear to cytoplasm translocation (PubMed:16300740).
Interacts with RNF2 (PubMed:28720707).
Interacts with FOXO3; this interaction represses FOXO3 transactivation (PubMed:20181828).
Interacts with PTMA; negatively regulates apoptotic process (PubMed:16478804).
Interacts with MYOD1, EP300 and DDX5; this interaction coordinates the association of anti-proliferative and pro-myogenic proteins at the myogenin promoter (By similarity) (PubMed:19723804).
Interacts with TP53; interaction is stress-dependent (PubMed:18690848).
Forms a complex with EP300 and TP53; this complex binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848).
Interacts with EP300; this interaction enhances the effect of EP300 on PAX2 transcription factor activity (PubMed:11940591).
Interacts with PAXIP1; this interaction prevents PAXIP1 inhibition of PAX2 transcription factor activity (PubMed:11940591).
Interacts with COPS5; this interaction allows COPS5-dependent CDKN1B nuclear to cytoplasm translocation (PubMed:16300740).
Interacts with RNF2 (PubMed:28720707).
Interacts with FOXO3; this interaction represses FOXO3 transactivation (PubMed:20181828).
Interacts with PTMA; negatively regulates apoptotic process (PubMed:16478804).
Interacts with MYOD1, EP300 and DDX5; this interaction coordinates the association of anti-proliferative and pro-myogenic proteins at the myogenin promoter (By similarity) (PubMed:19723804).
Interacts with TP53; interaction is stress-dependent (PubMed:18690848).
Forms a complex with EP300 and TP53; this complex binds CDKN1A promoter leading to transcriptional induction of CDKN1A (PubMed:18690848).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O60356 | CAPN2 P17655 | 3 | EBI-3908808, EBI-1028956 | |
BINARY | O60356 | CFAP100 Q494V2-2 | 3 | EBI-3908808, EBI-11953200 | |
BINARY | O60356 | PER1 O15534 | 3 | EBI-3908808, EBI-2557276 | |
BINARY | O60356 | PTMA P06454 | 7 | EBI-3908808, EBI-2682091 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-82 | Disordered | ||||
Sequence: MATFPPATSAPQQPPGPEDEDSSLDESDLYSLAHSYLGGGGRKGRTKREAAANTNRPSPGGHERKLVTKLQNSERKKRGARR | ||||||
Motif | 65-82 | Nuclear localization signal | ||||
Sequence: KLVTKLQNSERKKRGARR |
Sequence similarities
Belongs to the NUPR family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O60356-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length82
- Mass (Da)8,873
- Last updated1998-08-01 v1
- Checksum596E342D10F87AF3
O60356-2
- Name2
- Differences from canonical
- 37-37: L → LGPLIMPMPTSPLTPALVT
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BS92 | H3BS92_HUMAN | NUPR1 | 43 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_053816 | 37 | in isoform 2 | |||
Sequence: L → LGPLIMPMPTSPLTPALVT | ||||||
Sequence conflict | 47 | in Ref. 3; BAG35071 | ||||
Sequence: K → N |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF069073 EMBL· GenBank· DDBJ | AAC19384.1 EMBL· GenBank· DDBJ | mRNA | ||
AF069074 EMBL· GenBank· DDBJ | AAC19385.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF135266 EMBL· GenBank· DDBJ | AAD49221.1 EMBL· GenBank· DDBJ | mRNA | ||
AK312135 EMBL· GenBank· DDBJ | BAG35071.1 EMBL· GenBank· DDBJ | mRNA | ||
BM792961 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BT006896 EMBL· GenBank· DDBJ | AAP35542.1 EMBL· GenBank· DDBJ | mRNA | ||
CR542144 EMBL· GenBank· DDBJ | CAG46941.1 EMBL· GenBank· DDBJ | mRNA | ||
AC002425 EMBL· GenBank· DDBJ | AAC05336.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC002425 EMBL· GenBank· DDBJ | AAC05335.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CH471279 EMBL· GenBank· DDBJ | EAW52274.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002434 EMBL· GenBank· DDBJ | AAH02434.1 EMBL· GenBank· DDBJ | mRNA |