NPM1
entrez
4869
canonical
uniprot
P06748
canonical
ensembl
ENSG00000181163
resolver
ensp
ENSP00000296930
resolver
ensp
ENSP00000341168
resolver
ensp
ENSP00000377408
resolver
ensp
ENSP00000428755
resolver
ensp
ENSP00000429485
resolver
ensp
ENSP00000503781
resolver
ensp
ENSP00000593529
resolver
ensp
ENSP00000743167
resolver
enst
ENST00000521672
resolver
enst
ENST00000677325
resolver
genesymbol
NPM1
resolver
genesymbol_syn
NPM
resolver
hgnc
HGNC:7910
resolver
uniprot
A0A0S2Z491
resolver
uniprot
A0A0S2Z4G7
resolver
uniprot
A0A140VJQ2
resolver
uniprot
A8K3N7
resolver
uniprot
B5BU00
resolver
uniprot
D3DQL6
resolver
uniprot
E5RI98
resolver
uniprot
P08693
resolver
uniprot
Q12826
resolver
uniprot
Q13440
resolver
uniprot
Q13441
resolver
uniprot
Q14115
resolver
uniprot
Q5EU94
resolver
uniprot
Q5EU95
resolver
uniprot
Q5EU96
resolver
uniprot
Q5EU97
resolver
uniprot
Q5EU98
resolver
uniprot
Q5EU99
resolver
uniprot
Q6V962
resolver
uniprot
Q8WTW5
resolver
uniprot
Q96AT6
resolver
uniprot
Q96DC4
resolver
uniprot
Q96EA5
resolver
uniprot
Q9BYG9
resolver
uniprot
Q9UDJ7
resolver
uniprot_entry
A0A0S2Z491_HUMAN
resolver
uniprot_entry
A0A0S2Z4G7_HUMAN
resolver
uniprot_entry
A0A140VJQ2_HUMAN
resolver
uniprot_entry
E5RI98_HUMAN
resolver
uniprot_entry
NPM_HUMAN
resolver
uniprot_sec
A8K3N7
resolver
uniprot_sec
B5BU00
resolver
uniprot_sec
D3DQL6
resolver
uniprot_sec
P08693
resolver
uniprot_sec
Q12826
resolver
uniprot_sec
Q13440
resolver
uniprot_sec
Q13441
resolver
uniprot_sec
Q14115
resolver
uniprot_sec
Q5EU94
resolver
uniprot_sec
Q5EU95
resolver
uniprot_sec
Q5EU96
resolver
uniprot_sec
Q5EU97
resolver
uniprot_sec
Q5EU98
resolver
uniprot_sec
Q5EU99
resolver
uniprot_sec
Q6V962
resolver
uniprot_sec
Q8WTW5
resolver
uniprot_sec
Q96AT6
resolver
uniprot_sec
Q96DC4
resolver
uniprot_sec
Q96EA5
resolver
uniprot_sec
Q9BYG9
resolver
uniprot_sec
Q9UDJ7
resolver
amino_acid_sequence
MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEEEEDVKLLSISGKRSAPGGGSKVPQKKVKLAADEDDDDDDEEDDDEDDDDDDFDDEEAEEKAPVKKSIRDTPAKNAQKSNQNGKDSKPSSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated. {ECO:0000269|PubMed:8122112, ECO:0000269|PubMed:8633037}.; DISEASE: Note=A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA. {ECO:0000269|PubMed:8562957}.; DISEASE: Note=A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1. {ECO:0000269|PubMed:8570204}.; DISEASE: Note=Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location. {ECO:0000269|PubMed:15659725}.
uniprot
proteins
function
FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Antagonizes the inhibitory effect of ATF5 on cell proliferation and relieves ATF5-induced G2/M blockade (PubMed:22528486). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029). May act as chaperonin or cotransporter in the nucleolar localization of transcription termination factor TTF1 (By similarity). {ECO:0000250|UniProtKB:Q61937, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:16107701, ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:18809582, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:20352051, ECO:0000269|PubMed:21084279, ECO:0000269|PubMed:22002061, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25956029}.
uniprot
proteins
mass_dalton
32575
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="S->A: Abolishes phosphorylation by PLK2 and impairs centriole duplication."; /evidence="ECO:0000269|PubMed:20352051"; MUTAGEN 4; /note="S->D,E: Mimicks phosphorylation state, inducing accumulation of centrioles."; /evidence="ECO:0000269|PubMed:20352051"; MUTAGEN 95; /note="T->A: Does not affect phosphorylation by PLK2."; /evidence="ECO:0000269|PubMed:20352051"; MUTAGEN 125; /note="S->A: Does not affect phosphorylation by PLK2."; /evidence="ECO:0000269|PubMed:20352051"; MUTAGEN 199; /note="T->A: Partial loss of phosphorylation. Does not affect phosphorylation by PLK2."; /evidence="ECO:0000269|PubMed:12058066, ECO:0000269|PubMed:20352051"; MUTAGEN 219; /note="T->A: Partial loss of phosphorylation."; /evidence="ECO:0000269|PubMed:12058066"; MUTAGEN 234; /note="T->A: Partial loss of phosphorylation; when associated with A-237."; /evidence="ECO:0000269|PubMed:12058066"; MUTAGEN 237; /note="T->A: Partial loss of phosphorylation."; /evidence="ECO:0000269|PubMed:12058066"; MUTAGEN 248; /note="K->A: Partial destabilization of the structure."; /evidence="ECO:0000269|PubMed:18511415"; MUTAGEN 250; /note="K->A: Increase in the stabilization of the structure."; /evidence="ECO:0000269|PubMed:18511415"; MUTAGEN 263; /note="K->A: Increase in the stabilization of the structure and partial delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-267."; /evidence="ECO:0000269|PubMed:18259216"; MUTAGEN 263; /note="K->R: No change in the sumoylation level."; /evidence="ECO:0000269|PubMed:18259216"; MUTAGEN 267; /note="K->A: Increase in the stabilization of the structure and complete delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-263."; /evidence="ECO:0000269|PubMed:18511415"; MUTAGEN 268; /note="F->A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-276."; /evidence="ECO:0000269|PubMed:18511415"; MUTAGEN 276; /note="F->A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-268."; /evidence="ECO:0000269|PubMed:18511415"; MUTAGEN 288; /note="W->A: Complete destabilization of the structure; when associated with A-290."; /evidence="ECO:0000269|PubMed:18511415"; MUTAGEN 290; /note="W->A: Partial destabilization of the structure. Complete destabilization of the structure; when associated with A-288."; /evidence="ECO:0000269|PubMed:18511415
uniprot
proteins
post_translational_modification
PTM: Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. {ECO:0000269|PubMed:16107701, ECO:0000269|Ref.17}.; PTM: ADP-ribosylated.; PTM: 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. Phosphorylated by CDK2 at Ser-125 and Thr-199. Phosphorylation at Thr-199 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-199, Thr-219, Thr-234 and Thr-237 during cell mitosis. When these four sites are phosphorylated, RNA-binding activity seem to be abolished. May be phosphorylated at Ser-70 by NEK2. The Thr-199 phosphorylated form has higher affinity for ROCK2. CDK6 triggers Thr-199 phosphorylation when complexed to Kaposi's sarcoma herpesvirus (KSHV) V-cyclin, leading to viral reactivation by reducing viral LANA levels. {ECO:0000269|PubMed:11051553, ECO:0000269|PubMed:12058066, ECO:0000269|PubMed:12882984, ECO:0000269|PubMed:15190079, ECO:0000269|PubMed:15388344, ECO:0000269|PubMed:20333249, ECO:0000269|PubMed:20352051, ECO:0000269|Ref.17}.; PTM: Sumoylated by ARF. {ECO:0000269|PubMed:15897463}.; PTM: Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36 (PubMed:19208757). {ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:25818168}.
uniprot
proteins
protein_family
Nucleoplasmin family
uniprot
proteins
pubmed
11051553
uniprot
proteins
pubmed
11309377
uniprot
proteins
pubmed
12058066
uniprot
proteins
pubmed
12214246
uniprot
proteins
pubmed
12429849
uniprot
proteins
pubmed
12882984
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15190079
uniprot
proteins
pubmed
15388344
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15659725
uniprot
proteins
pubmed
15772089
uniprot
proteins
pubmed
15897463
uniprot
proteins
pubmed
16107701
uniprot
proteins
pubmed
16574551
uniprot
proteins
pubmed
16916647
uniprot
proteins
pubmed
17015463
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17215513
uniprot
proteins
pubmed
17879352
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18024471
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18259216
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18511415
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18809582
uniprot
proteins
pubmed
19015314
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19188445
uniprot
proteins
pubmed
19208757
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19710015
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20075868
uniprot
proteins
pubmed
20159986
uniprot
proteins
pubmed
20333249
uniprot
proteins
pubmed
20352051
uniprot
proteins
pubmed
20926688
uniprot
proteins
pubmed
21084279
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22002061
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22362753
uniprot
proteins
pubmed
22528486
uniprot
proteins
pubmed
23019224
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23972994
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2429957
uniprot
proteins
pubmed
2478125
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
25818168
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25956029
uniprot
proteins
pubmed
2602120
uniprot
proteins
pubmed
2713355
uniprot
proteins
pubmed
2775293
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28190768
uniprot
proteins
pubmed
28589727
uniprot
proteins
pubmed
38231884
uniprot
proteins
pubmed
3944116
uniprot
proteins
pubmed
7631008
uniprot
proteins
pubmed
8089149
uniprot
proteins
pubmed
8122112
uniprot
proteins
pubmed
8314759
uniprot
proteins
pubmed
8562957
uniprot
proteins
pubmed
8570204
uniprot
proteins
pubmed
8633037
uniprot
proteins
pubmed
9092633
uniprot
proteins
pubmed
9150948
uniprot
proteins
sequence_length
294
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:19208757, ECO:0000269|PubMed:22528486, ECO:0000269|PubMed:25818168, ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:28589727}. Nucleus, nucleoplasm {ECO:0000269|PubMed:25818168}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found in the cytoplasm in patients with primary acute myelogenous leukemia (AML), but not with secondary AML. Co-localizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for its localization to the centrosome during mitosis. Can shuttle between cytoplasm and nucleus (PubMed:38231884). {ECO:0000269|PubMed:38231884}.
uniprot
proteins