| + |
PLK1 | up-regulates 
phosphorylation
|
NPM1 |
0.435 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125666 |
Ser4 |
sMDMDMSP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15190079 |
Phosphorylated at ser-4 by plk1 and plk2. Phosphorylation at ser-4 by plk2 in s phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at ser-4 by plk1 takes place during mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK2 | up-regulates
phosphorylation
|
NPM1 |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125720 |
Ser4 |
sMDMDMSP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15190079 |
Phosphorylated at ser-4 by plk1 and plk2. Phosphorylation at ser-4 by plk2 in s phase is required for centriole duplication and is sufficient to trigger centriole replication. Phosphorylation at ser-4 by plk1 takes place during mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | down-regulates activity 
phosphorylation
|
NPM1 |
0.551 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276667 |
Ser48 |
QLSLRTVsLGAGAKD |
Homo sapiens |
T-24 Cell |
| pmid |
sentence |
| 25071014 |
We find that AKT phosphorylation of NPM-Ser48 prevents oligomerization that results in nucleoplasmic localization of ARF, constitutive MDM2 inhibition and stabilization of p53. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 |
phosphorylation
|
NPM1 |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161805 |
Ser70 |
EAMNYEGsPIKVTLA |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 19933706 |
Simultaneous inactivation of two cdk phosphorylation sites at ser10 and ser70 (npm-aa) induced g(2)/m cell cycle arrest, phosphorylation of cdk1 at tyr15 (cdc2(tyr15)) and increased cytoplasmic accumulation of cdc25c. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK1 |
phosphorylation
|
NPM1 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161801 |
Ser70 |
EAMNYEGsPIKVTLA |
Homo sapiens |
|
| pmid |
sentence |
| 19933706 |
Simultaneous inactivation of two cdk phosphorylation sites at ser10 and ser70 (npm-aa) induced g(2)/m cell cycle arrest, phosphorylation of cdk1 at tyr15 (cdc2(tyr15)) and increased cytoplasmic accumulation of cdc25c. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia |
| + |
CyclinE/CDK2 | down-regulates activity
phosphorylation
|
NPM1 |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250744 |
Thr199 |
VKKSIRDtPAKNAQK |
|
|
| pmid |
sentence |
| 11278991 |
Here, we identified that threonine 199 (Thr(199)) of NPM/B23 is the major phosphorylation target site of CDK2-cyclin E in vitro, and the same site is phosphorylated in vivo.|NPM/B23 binds specifically to unduplicated centrosomes and loses its centrosome binding activity when phosphorylated by CDK2-cyclin E |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216690 |
Thr234 |
SFKKQEKtPKTPKGP |
Homo sapiens |
|
| pmid |
sentence |
| 14670079 |
We have recently found that nucleophosmin (npm/b23), a phosphoprotein primarily found in nucleolus, associates with unduplicated centrosomes and is a direct substrate of cdk2-cyclin e in centrosome duplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216662 |
Thr234 |
SFKKQEKtPKTPKGP |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216674 |
Thr234 |
SFKKQEKtPKTPKGP |
Homo sapiens |
|
| pmid |
sentence |
| 11278991 |
We have recently found that nucleophosmin (npm/b23), a phosphoprotein primarily found in nucleolus, associates with unduplicated centrosomes and is a direct substrate of cdk2-cyclin e in centrosome duplication. |
|
| Publications: |
4 |
Organism: |
, Homo Sapiens |
| + |
CyclinB/CDK1 | down-regulates activity
phosphorylation
|
NPM1 |
0.418 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216845 |
Thr199 |
VKKSIRDtPAKNAQK |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
However, under the experimental conditions used here, the t199 residue was the most likely candidate to be phosphorylated by cyclin b/cdc2 these results strongly support the concept that the rna binding activity of b23.1 is inactivated by cyclin b/cdc2-mediated phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216745 |
Thr234 |
SFKKQEKtPKTPKGP |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216749 |
Thr237 |
KQEKTPKtPKGPSSV |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates activity
phosphorylation
|
NPM1 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89605 |
Thr199 |
VKKSIRDtPAKNAQK |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
However, under the experimental conditions used here, the t199 residue was the most likely candidate to be phosphorylated by cyclin b/cdc2 these results strongly support the concept that the rna binding activity of b23.1 is inactivated by cyclin b/cdc2-mediated phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120330 |
Thr234 |
SFKKQEKtPKTPKGP |
Homo sapiens |
|
| pmid |
sentence |
| 14670079 |
We have recently found that nucleophosmin (npm/b23), a phosphoprotein primarily found in nucleolus, associates with unduplicated centrosomes and is a direct substrate of cdk2-cyclin e in centrosome duplication. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235530 |
Thr234 |
SFKKQEKtPKTPKGP |
Mus musculus |
|
| pmid |
sentence |
| 11278991 |
CDK1-cyclin B phosphorylates NPM/B23 on Thr234. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89597 |
Thr234 |
SFKKQEKtPKTPKGP |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-120334 |
Thr237 |
KQEKTPKtPKGPSSV |
Homo sapiens |
|
| pmid |
sentence |
| 14670079 |
We further demonstrate that phospho-mkk1/mkk2 antibodies recognize npm on the c-terminal region, which is phosphorylated by cdc2 (cell division control kinase-2) during g2/m-phase. biochemical and immunocytochemistry analyses verified that the phospho-mkk1/mkk2 antibodies cross-reacted with npm that was phosphorylated at thr234 and thr237 during g2/m-phase, which are the same sites that are targeted by cdc2 (cell division cycle protein-2) during mitosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89601 |
Thr237 |
KQEKTPKtPKGPSSV |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens, Mus Musculus |
| Pathways: | Acute Myeloid Leukemia |
| + |
CDK2 | down-regulates activity
phosphorylation
|
NPM1 |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89609 |
Thr234 |
SFKKQEKtPKTPKGP |
Homo sapiens |
|
| pmid |
sentence |
| 12058066 |
Both subtypes of B23 proteins were phosphorylated during mitosis by cyclin B/cdc2. The RNA binding activity of B23.1 was repressed through cyclin B/cdc2-mediated phosphorylation at specific sites in B23. Thus, the RNA binding activity of B23.1 is stringently modulated by its phosphorylation and subtype association. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-235725 |
Thr234 |
SFKKQEKtPKTPKGP |
Mus musculus |
|
| pmid |
sentence |
| 11278991 |
We have recently found that nucleophosmin (npm/b23), a phosphoprotein primarily found in nucleolus, associates with unduplicated centrosomes and is a direct substrate of cdk2-cyclin e in centrosome duplication. Upon phosphorylation by CDK2-cyclin E, NPM/B23 dissociates from centrosomes, which is a prerequisite step for centrosomes to initiate duplication. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens, Mus Musculus |
| + |
USP36 | up-regulates quantity by stabilization
deubiquitination
|
NPM1 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272290 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19208757 |
USP36 deubiquitylated the nucleolar proteins nucleophosmin/B23 and fibrillarin, and stabilized them by counteracting ubiquitylation-mediated proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDKN2A | down-regulates quantity by destabilization
binding
|
NPM1 |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245077 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14636574 |
The Arf-NPM interaction seems to be critical in regulating the stability of both proteins. Arf, in fact, induces polyubiquitination and degradation of NPM and inhibits its effects on ribogenesis (18). NPM, instead, protects Arf from degradation and, surprisingly, antagonizes its ability to inhibit cell division |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, Onco-fusion proteins in AML, NPM1 in AML, AML_TRIPLETS, Triple mutant AML, NPM1_new |
| + |
NPM1 | down-regulates quantity by repression
transcriptional regulation
|
FBP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267594 |
|
|
Homo sapiens |
Pancreatic Ductal Adenocarcinoma Cell, Melanoma Cell Line |
| pmid |
sentence |
| 30616754 |
For instance, nucleophosmin (NPM1) and zinc-finger protein X-linked (ZFX) bind to the E-box and ZFX binding site on the FBP1 promoter, respectively, and restrain FBP1 expression to facilitate aerobic glycolysis in PDAC and melanoma |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NPM1 | down-regulates quantity by repression
transcriptional regulation
|
HOXA9 |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260138 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30205049 |
In AML cells, NPM1 mutations result in abnormal cytoplasmic localization of the mutant protein (NPM1c); however, it is unknown whether NPM1c is required to maintain the leukemic state. Here, we show that loss of NPM1c from the cytoplasm, either through nuclear relocalization or targeted degradation, results in immediate downregulation of homeobox (HOX) genes followed by differentiation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, Onco-fusion proteins in AML, AML_TRIPLETS, Triple mutant AML |
| + |
NPM1 | up-regulates activity
binding
|
CENPA |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263708 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19410544 |
Here we demonstrate that prenucleosomal CENP-A is complexed with histone H4, nucleophosmin 1, and HJURPA minority of NPM1 cofractionated with prenucleosomal CENP-A, consistent with only a small proportion of total NPM1 stably associated with CENP-A. The partial overlap of NPM1 and HJURP with each other supports their formation of distinct prenucleosomal complexes with CENP-A. it is also possible that NPM1 plays a non essential role in the assembly of CENP-A nucleosomes or the nucleophosmin paralogues NPM2 and NPM3 may compensate for the absence of NPM1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NPM1 | up-regulates activity
binding
|
CDKN2A |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245073 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 16199867 |
The Arf-NPM interaction seems to be critical in regulating the stability of both proteins. Arf, in fact, induces polyubiquitination and degradation of NPM and inhibits its effects on ribogenesis (18). NPM, instead, protects Arf from degradation and, surprisingly, antagonizes its ability to inhibit cell division |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, Onco-fusion proteins in AML, NPM1 in AML, AML_TRIPLETS, Triple mutant AML, NPM1_new |
| + |
NPM1 | down-regulates activity
binding
|
HEXIM1 |
0.395 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260134 |
|
|
Homo sapiens |
Acute Myeloid Leukemia Cell |
| pmid |
sentence |
| 18371977 |
We identified NPM as a novel HEXIM1-binding protein. NPM functioned as a negative regulator of HEXIM1. cytoplasmic localization of endogenous HEXIM1 is detected in an acute myeloid leukemia (AML) cell line containing the NPMc+ mutation, suggesting the physiological importance of HEXIM1-NPMc+ interaction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NPM1 | up-regulates quantity
binding
|
FBXW7 |
0.496 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-245084 |
|
|
Mus musculus |
MEF Cell |
| pmid |
sentence |
| 18625840 |
We report here that NPM regulates turnover of the c-Myc oncoprotein by acting on the F-box protein Fbw7 , a component of the E3 ligase complex involved in the ubiquitination and proteasome degradation of c-Myc. NPM was required for nucleolar localization and stabili- zation of Fbw7 |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | Acute Myeloid Leukemia, DNMT3A in AML, NPM1 in AML, AML_TRIPLETS, Triple mutant AML, NPM1_new |
| + |
RNF144B | down-regulates quantity by destabilization
ubiquitination
|
NPM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271490 |
|
|
Homo sapiens |
Lymphoblast |
| pmid |
sentence |
| 20864535 |
NPMc degradation was mediated by the ubiquitin-proteasome pathway involving the IBR-type RING-finger E3 ubiquitin ligase IBRDC2, and genetic correction of FA-A or FA-C lymphoblasts prevented NPMc ubiquitination. As shown in Fig. 4C, knockdown of IBRDC2, an IBR-type RING-finger E3 ubiquitin ligase (21), significantly reduced NPMc ubiquitination and restored NPMc stability in FA-A cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP3 | down-regulates activity
dephosphorylation
|
NPM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277005 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33777934 |
In the absence of DUSP3, these three residues remain phosphorylated and favor the dissociation equilibrium of NPM homo-oligomerization and/or its association with ARF, therefore promoting an early nuc|Therefore, here we focused on the molecular mechanisms used by DUSP3-NPM interaction to affect the abovementioned cellular responses and found out that DUSP3 dephosphorylates three tyrosine residues (Y29, Y67, and Y271) of NPM. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NPM1
- 
- 