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Protein

Nucleophosmin

Gene

NPM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).9 Publications

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein kinase inhibitor activity Source: UniProtKB
  • ribosomal large subunit binding Source: MGI
  • ribosomal small subunit binding Source: MGI
  • RNA binding Source: UniProtKB
  • Tat protein binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • cell aging Source: UniProtKB
  • CENP-A containing nucleosome assembly Source: Reactome
  • centrosome cycle Source: UniProtKB
  • DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  • DNA repair Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of centrosome duplication Source: UniProtKB
  • negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  • nucleocytoplasmic transport Source: UniProtKB
  • nucleosome assembly Source: UniProtKB
  • positive regulation of cell cycle G2/M phase transition Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of translation Source: UniProtKB
  • protein localization Source: UniProtKB
  • protein oligomerization Source: MGI
  • regulation of centriole replication Source: UniProtKB
  • regulation of eIF2 alpha phosphorylation by dsRNA Source: UniProtKB
  • regulation of endodeoxyribonuclease activity Source: UniProtKB
  • regulation of endoribonuclease activity Source: UniProtKB
  • response to stress Source: UniProtKB
  • ribosome assembly Source: UniProtKB
  • signal transduction Source: UniProtKB
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000181163-MONOMER.
ReactomeiR-HSA-180746. Nuclear import of Rev protein.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
R-HSA-8869496. TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
SIGNORiP06748.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleophosmin
Short name:
NPM
Alternative name(s):
Nucleolar phosphoprotein B23
Nucleolar protein NO38
Numatrin
Gene namesi
Name:NPM1
Synonyms:NPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:7910. NPM1.

Subcellular locationi

  • Nucleusnucleolus 1 Publication
  • Nucleusnucleoplasm
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome

  • 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. Can shuttle between cytoplasm and nucleus. 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.

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • focal adhesion Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: MGI
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • spindle pole centrosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA.

A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1.

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4S → A: Abolishes phosphorylation by PLK2 and impairs centriole duplication. 1 Publication1
Mutagenesisi4S → D or E: Mimicks phosphorylation state, inducing accumulation of centrioles. 1 Publication1
Mutagenesisi95T → A: Does not affect phosphorylation by PLK2. 1 Publication1
Mutagenesisi125S → A: Does not affect phosphorylation by PLK2. 1 Publication1
Mutagenesisi199T → A: Partial loss of phosphorylation. Does not affect phosphorylation by PLK2. 2 Publications1
Mutagenesisi219T → A: Partial loss of phosphorylation. 1 Publication1
Mutagenesisi234T → A: Partial loss of phosphorylation; when associated with A-237. 1 Publication1
Mutagenesisi237T → A: Partial loss of phosphorylation. 1 Publication1
Mutagenesisi248K → A: Partial destabilization of the structure. 1 Publication1
Mutagenesisi250K → A: Increase in the stabilization of the structure. 1 Publication1
Mutagenesisi263K → A: Increase in the stabilization of the structure and partial delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-267. 1 Publication1
Mutagenesisi263K → R: No change in the sumoylation level. 1 Publication1
Mutagenesisi267K → A: Increase in the stabilization of the structure and complete delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-263. 1
Mutagenesisi268F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-276. 1 Publication1
Mutagenesisi276F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-268. 1 Publication1
Mutagenesisi288W → A: Complete destabilization of the structure; when associated with A-290. 1 Publication1
Mutagenesisi290W → A: Partial destabilization of the structure. Complete destabilization of the structure; when associated with A-288. 1 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei175 – 176Breakpoint for translocation to form NPM1-MLF11 Publication2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi4869.
MalaCardsiNPM1.
OpenTargetsiENSG00000181163.
Orphaneti98834. Acute myeloblastic leukemia with maturation.
98833. Acute myeloblastic leukemia without maturation.
402026. Acute myeloid leukemia with NPM1 somatic mutations.
520. Acute promyelocytic leukemia.
PharmGKBiPA31712.

Chemistry databases

ChEMBLiCHEMBL5178.

Polymorphism and mutation databases

BioMutaiNPM1.
DMDMi114762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194811 – 294NucleophosminAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei4Phosphoserine; by PLK1 and PLK2Combined sources2 Publications1
Modified residuei10PhosphoserineCombined sources1
Cross-linki27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei32N6-acetyllysine; alternateCombined sources1
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei43PhosphoserineCombined sources1
Modified residuei70PhosphoserineCombined sources1
Modified residuei75PhosphothreonineCombined sources1
Modified residuei95PhosphothreonineCombined sources1
Modified residuei125Phosphoserine; by CDK2Combined sources1 Publication1
Modified residuei137PhosphoserineCombined sources1
Modified residuei139PhosphoserineCombined sources1
Modified residuei150N6-acetyllysineCombined sources1
Modified residuei154N6-acetyllysineCombined sources1
Modified residuei199Phosphothreonine; by CDK1, CDK2 and CDK6Combined sources2 Publications1
Modified residuei212N6-acetyllysineCombined sources1 Publication1
Cross-linki215Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei219Phosphothreonine; by CDK11 Publication1
Modified residuei227PhosphoserineCombined sources1
Modified residuei229N6-acetyllysine1 Publication1
Modified residuei230N6-acetyllysine; alternate1 Publication1
Cross-linki230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei234Phosphothreonine; by CDK1Combined sources1
Modified residuei237Phosphothreonine; by CDK1Combined sources1 Publication1
Modified residuei242PhosphoserineCombined sources1
Modified residuei243PhosphoserineCombined sources1
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei250N6-acetyllysine; alternate1 Publication1
Cross-linki250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei254PhosphoserineCombined sources1
Modified residuei257N6-acetyllysine; alternateCombined sources1 Publication1
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei260PhosphoserineCombined sources1
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei267N6-acetyllysine; alternateCombined sources1
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Modified residuei273N6-acetyllysineCombined sources1
Modified residuei279PhosphothreonineCombined sources1
Modified residuei292N6-acetyllysine1 Publication1
Isoform 3 (identifier: P06748-3)
Modified residuei254PhosphoserineCombined sources1
Modified residuei257N6-acetyllysineCombined sources1

Post-translational modificationi

Acetylated at C-terminal lysine residues, thereby increasing affinity to histones.2 Publications
ADP-ribosylated.
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 phosphorated, 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.8 Publications
Sumoylated by ARF.1 Publication

Keywords - PTMi

Acetylation, ADP-ribosylation, Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP06748.
MaxQBiP06748.
PaxDbiP06748.
PeptideAtlasiP06748.
PRIDEiP06748.
TopDownProteomicsiP06748-1. [P06748-1]
P06748-2. [P06748-2]
P06748-3. [P06748-3]

2D gel databases

DOSAC-COBS-2DPAGEP06748.
REPRODUCTION-2DPAGEIPI00549248.
SWISS-2DPAGEP06748.

PTM databases

iPTMnetiP06748.
PhosphoSitePlusiP06748.
SwissPalmiP06748.

Miscellaneous databases

PMAP-CutDBP06748.

Expressioni

Gene expression databases

BgeeiENSG00000181163.
ExpressionAtlasiP06748. baseline and differential.
GenevisibleiP06748. HS.

Organism-specific databases

HPAiCAB012983.
HPA011384.
HPA053413.

Interactioni

Subunit structurei

Decamer formed by two pentameric rings associated in a head-to-head fashion. Disulfide-linked dimers under certain conditions. The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (By similarity). Interacts with NSUN2 and SENP3. Interacts with hepatitis delta virus S-HDAg. Interacts with HTLV1 Rex protein (via N-terminal nuclear localization signal). Interacts with the methylated form of RPS10. Interacts (via N-terminal domain) with APEX1; the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts with isoform 1 of NEK2. Interacts with ROCK2 and BRCA2. Interacts with RPGR. Interacts with CENPW. Interacts with EIF2AK2/PKR. Interacts with CEBPA (isoform 4) (PubMed:20075868). Interacts with DDX31; this interaction prevents interaction between NPM1 and HDM2 (PubMed:23019224).By similarity16 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei55Interaction between pentamersBy similarity1
Sitei80Interaction between pentamersBy similarity1

Binary interactionsi

WithEntry#Exp.IntActNotes
Q981472EBI-78579,EBI-626601From a different organism.
AURKAO149653EBI-78579,EBI-448680
AURKBQ96GD45EBI-78579,EBI-624291
CDKN2AQ8N7262EBI-78579,EBI-625922
COX8AP101763EBI-78579,EBI-3904738
CPSF1Q105702EBI-78579,EBI-347859
EIF2AK2P195253EBI-78579,EBI-640775
FAM129AQ9BZQ87EBI-78579,EBI-6916466
HDAC1Q135472EBI-78579,EBI-301834
HDAC2Q927692EBI-78579,EBI-301821
HEMGNQ9BXL57EBI-78579,EBI-3916399
L2P249384EBI-78579,EBI-7481199From a different organism.
L2P689515EBI-78579,EBI-7481182From a different organism.
MP034193EBI-78579,EBI-10042882From a different organism.
MDM2Q009875EBI-78579,EBI-389668
NPM2Q86SE85EBI-78579,EBI-6658150
PELP1Q8IZL83EBI-78579,EBI-716449
pre-C/CB1Q2W98EBI-78579,EBI-9081051From a different organism.
SENP3Q9H4L46EBI-78579,EBI-2880236
TFAP2AP055496EBI-78579,EBI-347351
TP53P046376EBI-78579,EBI-366083
YWHAZP631042EBI-78579,EBI-347088

GO - Molecular functioni

  • histone binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • Tat protein binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110929. 580 interactors.
DIPiDIP-30932N.
IntActiP06748. 258 interactors.
MINTiMINT-4938330.
STRINGi9606.ENSP00000296930.

Chemistry databases

BindingDBiP06748.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi16 – 19Combined sources4
Beta strandi29 – 31Combined sources3
Beta strandi41 – 49Combined sources9
Beta strandi58 – 65Combined sources8
Beta strandi69 – 80Combined sources12
Turni81 – 83Combined sources3
Beta strandi84 – 94Combined sources11
Beta strandi96 – 105Combined sources10
Beta strandi109 – 116Combined sources8
Helixi244 – 257Combined sources14
Helixi265 – 275Combined sources11
Helixi281 – 292Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LLHNMR-A225-294[»]
2P1BX-ray2.75A/B/C/D/E/F/G/H/I/J9-122[»]
2VXDNMR-A243-294[»]
ProteinModelPortaliP06748.
SMRiP06748.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06748.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 186Required for interaction with SENP3Add BLAST186
Regioni1 – 117Necessary for interaction with APEX11 PublicationAdd BLAST117
Regioni243 – 294Required for nucleolar localizationAdd BLAST52

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi152 – 157Nuclear localization signalSequence analysis6
Motifi191 – 197Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 9Met-rich9
Compositional biasi120 – 132Asp/Glu-rich (acidic)Add BLAST13
Compositional biasi161 – 188Asp/Glu-rich (highly acidic)Add BLAST28

Sequence similaritiesi

Belongs to the nucleoplasmin family.Curated

Phylogenomic databases

eggNOGiENOG410IHZM. Eukaryota.
ENOG4111IKX. LUCA.
GeneTreeiENSGT00440000034554.
HOGENOMiHOG000013061.
HOVERGENiHBG001860.
InParanoidiP06748.
KOiK11276.
OMAiVEACICS.
OrthoDBiEOG091G0NLY.
PhylomeDBiP06748.
TreeFamiTF327704.

Family and domain databases

Gene3Di2.60.120.340. 1 hit.
InterProiIPR032569. NPM1_C.
IPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERiPTHR22747. PTHR22747. 1 hit.
PfamiPF16276. NPM1-C. 1 hit.
PF03066. Nucleoplasmin. 1 hit.
[Graphical view]
SUPFAMiSSF69203. SSF69203. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P06748-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG
60 70 80 90 100
AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL
110 120 130 140 150
RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK
160 170 180 190 200
VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP
210 220 230 240 250
AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK
260 270 280 290
MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL
Length:294
Mass (Da):32,575
Last modified:November 1, 1990 - v2
Checksum:i620BC7BA2E4A0054
GO
Isoform 2 (identifier: P06748-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-223: Missing.

Show »
Length:265
Mass (Da):29,465
Checksum:i932BEC3377692D91
GO
Isoform 3 (identifier: P06748-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     258-294: GGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL → AH

Show »
Length:259
Mass (Da):28,400
Checksum:i6AEAD2909EE0A47A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti80K → E in AAH21983 (PubMed:15489334).Curated1
Sequence conflicti129E → D AA sequence (PubMed:3944116).Curated1
Sequence conflicti168Missing in AAW67758 (PubMed:15659725).Curated1
Sequence conflicti178D → G in AAH16768 (PubMed:15489334).Curated1
Sequence conflicti183D → N in BAG70175 (PubMed:19054851).Curated1
Sequence conflicti183D → N in BAG70050 (PubMed:19054851).Curated1
Sequence conflicti213D → P in AAA36473 (PubMed:2429957).Curated1
Sequence conflicti213D → P in AAA36474 (PubMed:2429957).Curated1
Sequence conflicti214S → L AA sequence (PubMed:12882984).Curated1
Sequence conflicti216P → S in AAA36473 (PubMed:2429957).Curated1
Sequence conflicti219 – 221TPR → SSS in AAA36473 (PubMed:2429957).Curated3
Sequence conflicti231Q → R in AAQ24860 (Ref. 8) Curated1
Sequence conflicti271Y → C in AAH16768 (PubMed:15489334).Curated1
Sequence conflicti287L → F in AAH12566 (PubMed:15489334).Curated1
Sequence conflicti288 – 294WQWRKSL → CLAVEEVSLRK in AAW67752 (PubMed:15659725).Curated7
Sequence conflicti288 – 294WQWRKSL → CLAVEEVSLRK in AAW67755 (PubMed:15659725).Curated7
Sequence conflicti288 – 294WQWRKSL → CMAVEEVSLRK in AAW67753 (PubMed:15659725).Curated7
Sequence conflicti288 – 294WQWRKSL → CMAVEEVSLRK in ABC40399 (PubMed:16574551).Curated7
Sequence conflicti288 – 294WQWRKSL → CVAVEEVSLRK in AAW67754 (PubMed:15659725).Curated7
Sequence conflicti290 – 294WRKSL → SLAQVSLRK in AAW67756 (PubMed:15659725).Curated5
Sequence conflicti290 – 294WRKSL → SLEKVSLRK in AAW67757 (PubMed:15659725).Curated5

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003616195 – 223Missing in isoform 2. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_043599258 – 294GGSLP…WRKSL → AH in isoform 3. 2 PublicationsAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23613 mRNA. Translation: AAA36380.1.
M28699 mRNA. Translation: AAA58386.1.
M26697 mRNA. Translation: AAA36385.1.
U89321
, U89309, U89310, U89311, U89313, U89314, U89317, U89319 Genomic DNA. Translation: AAB94739.1.
AB042278 mRNA. Translation: BAB40600.1.
AY740634 mRNA. Translation: AAW67752.1.
AY740635 mRNA. Translation: AAW67753.1.
AY740636 mRNA. Translation: AAW67754.1.
AY740637 mRNA. Translation: AAW67755.1.
AY740638 mRNA. Translation: AAW67756.1.
AY740639 mRNA. Translation: AAW67757.1.
AY740640 mRNA. Translation: AAW67758.1.
DQ303464 mRNA. Translation: ABC40399.1.
AY347529 mRNA. Translation: AAQ24860.1.
BT007011 mRNA. Translation: AAP35657.1.
AK290652 mRNA. Translation: BAF83341.1.
AB451236 mRNA. Translation: BAG70050.1.
AB451361 mRNA. Translation: BAG70175.1.
CH471062 Genomic DNA. Translation: EAW61443.1.
CH471062 Genomic DNA. Translation: EAW61446.1.
BC002398 mRNA. Translation: AAH02398.1.
BC008495 mRNA. Translation: AAH08495.1.
BC009623 mRNA. Translation: AAH09623.1.
BC012566 mRNA. Translation: AAH12566.1.
BC014349 mRNA. Translation: AAH14349.1.
BC016716 mRNA. Translation: AAH16716.1.
BC016768 mRNA. Translation: AAH16768.1.
BC016824 mRNA. Translation: AAH16824.1.
BC021668 mRNA. Translation: AAH21668.1.
BC021983 mRNA. Translation: AAH21983.1.
BC050628 mRNA. Translation: AAH50628.1.
BC107754 mRNA. Translation: AAI07755.1.
U41742 mRNA. Translation: AAB00112.1. Different termination.
U41743 mRNA. Translation: AAB00113.1. Different termination.
U04946 mRNA. Translation: AAA58698.1. Different termination.
D45915 mRNA. Translation: BAA08343.1. Different termination.
X16934 mRNA. Translation: CAA34809.1.
J02590 mRNA. Translation: AAA36473.1.
M31004 mRNA. Translation: AAA36474.1.
CCDSiCCDS43399.1. [P06748-3]
CCDS4376.1. [P06748-1]
CCDS4377.1. [P06748-2]
PIRiA33423. A32915.
I38491.
RefSeqiNP_001032827.1. NM_001037738.2. [P06748-3]
NP_002511.1. NM_002520.6. [P06748-1]
NP_954654.1. NM_199185.3. [P06748-2]
UniGeneiHs.557550.

Genome annotation databases

EnsembliENST00000296930; ENSP00000296930; ENSG00000181163. [P06748-1]
ENST00000351986; ENSP00000341168; ENSG00000181163. [P06748-2]
ENST00000393820; ENSP00000377408; ENSG00000181163. [P06748-3]
ENST00000517671; ENSP00000428755; ENSG00000181163. [P06748-1]
GeneIDi4869.
KEGGihsa:4869.
UCSCiuc003mbh.4. human. [P06748-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23613 mRNA. Translation: AAA36380.1.
M28699 mRNA. Translation: AAA58386.1.
M26697 mRNA. Translation: AAA36385.1.
U89321
, U89309, U89310, U89311, U89313, U89314, U89317, U89319 Genomic DNA. Translation: AAB94739.1.
AB042278 mRNA. Translation: BAB40600.1.
AY740634 mRNA. Translation: AAW67752.1.
AY740635 mRNA. Translation: AAW67753.1.
AY740636 mRNA. Translation: AAW67754.1.
AY740637 mRNA. Translation: AAW67755.1.
AY740638 mRNA. Translation: AAW67756.1.
AY740639 mRNA. Translation: AAW67757.1.
AY740640 mRNA. Translation: AAW67758.1.
DQ303464 mRNA. Translation: ABC40399.1.
AY347529 mRNA. Translation: AAQ24860.1.
BT007011 mRNA. Translation: AAP35657.1.
AK290652 mRNA. Translation: BAF83341.1.
AB451236 mRNA. Translation: BAG70050.1.
AB451361 mRNA. Translation: BAG70175.1.
CH471062 Genomic DNA. Translation: EAW61443.1.
CH471062 Genomic DNA. Translation: EAW61446.1.
BC002398 mRNA. Translation: AAH02398.1.
BC008495 mRNA. Translation: AAH08495.1.
BC009623 mRNA. Translation: AAH09623.1.
BC012566 mRNA. Translation: AAH12566.1.
BC014349 mRNA. Translation: AAH14349.1.
BC016716 mRNA. Translation: AAH16716.1.
BC016768 mRNA. Translation: AAH16768.1.
BC016824 mRNA. Translation: AAH16824.1.
BC021668 mRNA. Translation: AAH21668.1.
BC021983 mRNA. Translation: AAH21983.1.
BC050628 mRNA. Translation: AAH50628.1.
BC107754 mRNA. Translation: AAI07755.1.
U41742 mRNA. Translation: AAB00112.1. Different termination.
U41743 mRNA. Translation: AAB00113.1. Different termination.
U04946 mRNA. Translation: AAA58698.1. Different termination.
D45915 mRNA. Translation: BAA08343.1. Different termination.
X16934 mRNA. Translation: CAA34809.1.
J02590 mRNA. Translation: AAA36473.1.
M31004 mRNA. Translation: AAA36474.1.
CCDSiCCDS43399.1. [P06748-3]
CCDS4376.1. [P06748-1]
CCDS4377.1. [P06748-2]
PIRiA33423. A32915.
I38491.
RefSeqiNP_001032827.1. NM_001037738.2. [P06748-3]
NP_002511.1. NM_002520.6. [P06748-1]
NP_954654.1. NM_199185.3. [P06748-2]
UniGeneiHs.557550.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LLHNMR-A225-294[»]
2P1BX-ray2.75A/B/C/D/E/F/G/H/I/J9-122[»]
2VXDNMR-A243-294[»]
ProteinModelPortaliP06748.
SMRiP06748.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110929. 580 interactors.
DIPiDIP-30932N.
IntActiP06748. 258 interactors.
MINTiMINT-4938330.
STRINGi9606.ENSP00000296930.

Chemistry databases

BindingDBiP06748.
ChEMBLiCHEMBL5178.

PTM databases

iPTMnetiP06748.
PhosphoSitePlusiP06748.
SwissPalmiP06748.

Polymorphism and mutation databases

BioMutaiNPM1.
DMDMi114762.

2D gel databases

DOSAC-COBS-2DPAGEP06748.
REPRODUCTION-2DPAGEIPI00549248.
SWISS-2DPAGEP06748.

Proteomic databases

EPDiP06748.
MaxQBiP06748.
PaxDbiP06748.
PeptideAtlasiP06748.
PRIDEiP06748.
TopDownProteomicsiP06748-1. [P06748-1]
P06748-2. [P06748-2]
P06748-3. [P06748-3]

Protocols and materials databases

DNASUi4869.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296930; ENSP00000296930; ENSG00000181163. [P06748-1]
ENST00000351986; ENSP00000341168; ENSG00000181163. [P06748-2]
ENST00000393820; ENSP00000377408; ENSG00000181163. [P06748-3]
ENST00000517671; ENSP00000428755; ENSG00000181163. [P06748-1]
GeneIDi4869.
KEGGihsa:4869.
UCSCiuc003mbh.4. human. [P06748-1]

Organism-specific databases

CTDi4869.
DisGeNETi4869.
GeneCardsiNPM1.
HGNCiHGNC:7910. NPM1.
HPAiCAB012983.
HPA011384.
HPA053413.
MalaCardsiNPM1.
MIMi164040. gene.
neXtProtiNX_P06748.
OpenTargetsiENSG00000181163.
Orphaneti98834. Acute myeloblastic leukemia with maturation.
98833. Acute myeloblastic leukemia without maturation.
402026. Acute myeloid leukemia with NPM1 somatic mutations.
520. Acute promyelocytic leukemia.
PharmGKBiPA31712.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHZM. Eukaryota.
ENOG4111IKX. LUCA.
GeneTreeiENSGT00440000034554.
HOGENOMiHOG000013061.
HOVERGENiHBG001860.
InParanoidiP06748.
KOiK11276.
OMAiVEACICS.
OrthoDBiEOG091G0NLY.
PhylomeDBiP06748.
TreeFamiTF327704.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000181163-MONOMER.
ReactomeiR-HSA-180746. Nuclear import of Rev protein.
R-HSA-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-HSA-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
R-HSA-8869496. TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation.
SIGNORiP06748.

Miscellaneous databases

ChiTaRSiNPM1. human.
EvolutionaryTraceiP06748.
GeneWikiiNPM1.
GenomeRNAii4869.
PMAP-CutDBP06748.
PROiP06748.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000181163.
ExpressionAtlasiP06748. baseline and differential.
GenevisibleiP06748. HS.

Family and domain databases

Gene3Di2.60.120.340. 1 hit.
InterProiIPR032569. NPM1_C.
IPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERiPTHR22747. PTHR22747. 1 hit.
PfamiPF16276. NPM1-C. 1 hit.
PF03066. Nucleoplasmin. 1 hit.
[Graphical view]
SUPFAMiSSF69203. SSF69203. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNPM_HUMAN
AccessioniPrimary (citable) accession number: P06748
Secondary accession number(s): A8K3N7
, B5BU00, D3DQL6, P08693, Q12826, Q13440, Q13441, Q14115, Q5EU94, Q5EU95, Q5EU96, Q5EU97, Q5EU98, Q5EU99, Q6V962, Q8WTW5, Q96AT6, Q96DC4, Q96EA5, Q9BYG9, Q9UDJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: November 30, 2016
This is version 209 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.