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Protein

Nucleophosmin

Gene

NPM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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). In complex with MYC enhances the transcription of MYC target genes (PubMed:25956029).10 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChaperone, RNA-binding
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-180746 Nuclear import of Rev protein
R-HSA-3899300 SUMOylation of transcription cofactors
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

SIGNOR Signaling Network Open Resource

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SIGNORi
P06748

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Nucleophosmin
Short name:
NPM
Alternative name(s):
Nucleolar phosphoprotein B23
Nucleolar protein NO38
Numatrin
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NPM1
Synonyms:NPM
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000181163.13

Human Gene Nomenclature Database

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HGNCi
HGNC:7910 NPM1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
164040 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P06748

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.2 Publications
A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA.1 Publication
A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1.1 Publication
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.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei175 – 176Breakpoint for translocation to form NPM1-MLF11 Publication2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
4869

MalaCards human disease database

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MalaCardsi
NPM1

Open Targets

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OpenTargetsi
ENSG00000181163

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
98834 Acute myeloblastic leukemia with maturation
98833 Acute myeloblastic leukemia without maturation
402026 Acute myeloid leukemia with NPM1 somatic mutations
520 Acute promyelocytic leukemia
98842 Lymphomatoid papulosis
300865 Primary cutaneous anaplastic large cell lymphoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA31712

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5178

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
NPM1

Domain mapping of disease mutations (DMDM)

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DMDMi
114762

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002194811 – 294NucleophosminAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei4Phosphoserine; by PLK1 and PLK2Combined sources2 Publications1
Modified residuei10PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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 residuei67PhosphotyrosineBy similarity1
Modified residuei70PhosphoserineCombined sources1
Modified residuei75PhosphothreonineCombined sources1
Modified residuei95PhosphothreonineCombined sources1
Modified residuei125Phosphoserine; by CDK2Combined sources1 Publication1
Modified residuei137PhosphoserineCombined sources1
Modified residuei139PhosphoserineCombined sources1
Cross-linki141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei150N6-acetyllysine; alternateCombined sources1
Cross-linki150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei154N6-acetyllysineCombined sources1
Modified residuei199Phosphothreonine; by CDK1, CDK2 and CDK6Combined sources2 Publications1
Modified residuei207ADP-ribosylserine1 Publication1
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); alternateCombined sources
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined 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); alternate1 Publication
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei267N6-acetyllysine; alternateCombined sources1
Modified residuei267N6-succinyllysine; alternateBy similarity1
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei273N6-acetyllysine; alternateCombined sources1
Cross-linki273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei279PhosphothreonineCombined sources1
Modified residuei292N6-acetyllysine1 Publication1
Isoform 3 (identifier: P06748-3)
Modified residuei254Phosphoserine1
Modified residuei257N6-acetyllysine1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
Ubiquitinated. Ubiquitination leads to proteasomal degradation. Deubiquitinated by USP36 (PubMed:19208757).2 Publications

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P06748

MaxQB - The MaxQuant DataBase

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MaxQBi
P06748

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P06748

PeptideAtlas

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PeptideAtlasi
P06748

PRoteomics IDEntifications database

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PRIDEi
P06748

ProteomicsDB human proteome resource

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ProteomicsDBi
51927
51928 [P06748-2]
51929 [P06748-3]

Consortium for Top Down Proteomics

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TopDownProteomicsi
P06748-1 [P06748-1]
P06748-2 [P06748-2]
P06748-3 [P06748-3]

2D gel databases

DOSAC-COBS 2D-PAGE database

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DOSAC-COBS-2DPAGEi
P06748

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
IPI00549248

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P06748

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P06748

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P06748

SwissPalm database of S-palmitoylation events

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SwissPalmi
P06748

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P06748

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000181163 Expressed in 215 organ(s), highest expression level in kidney

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P06748 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P06748 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB012983
HPA011384

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Decamer formed by two pentameric rings associated in a head-to-head fashion (By similarity). Disulfide-linked dimers under certain conditions (PubMed:25818168). The SWAP complex consists of NPM1, NCL, PARP1 and SWAP70 (By similarity). Interacts with NSUN2 and SENP3. 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). Interacts with MYC; competitive with NOP53 (PubMed:25956029). Interacts with NOP53; the interaction is direct and competitive with MYC (PubMed:25956029). Interacts with LRRC34 (By similarity). Interacts with RRP1B (PubMed:19710015, PubMed:20926688).By similarity18 Publications
(Microbial infection) Interacts with hepatitis delta virus S-HDAg.1 Publication
(Microbial infection) Interacts with HTLV1 Rex protein (via N-terminal nuclear localization signal).1 Publication

Sites

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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
110929, 597 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P06748

Database of interacting proteins

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DIPi
DIP-30932N

Protein interaction database and analysis system

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IntActi
P06748, 275 interactors

Molecular INTeraction database

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MINTi
P06748

STRING: functional protein association networks

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STRINGi
9606.ENSP00000296930

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P06748

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P06748

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P06748

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P06748

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi152 – 157Nuclear localization signalSequence analysis6
Motifi191 – 197Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 9Met-rich9
Compositional biasi120 – 132Asp/Glu-rich (acidic)Add BLAST13
Compositional biasi161 – 188Asp/Glu-rich (highly acidic)Add BLAST28

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the nucleoplasmin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IHZM Eukaryota
ENOG4111IKX LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153052

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000013061

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001860

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P06748

KEGG Orthology (KO)

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KOi
K11276

Identification of Orthologs from Complete Genome Data

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OMAi
VEACICS

Database of Orthologous Groups

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OrthoDBi
EOG091G0NLY

Database for complete collections of gene phylogenies

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PhylomeDBi
P06748

TreeFam database of animal gene trees

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TreeFami
TF327704

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.2100, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR032569 NPM1_C
IPR038101 NPM1_C_sf
IPR004301 Nucleoplasmin
IPR024057 Nucleoplasmin_core_dom
IPR036824 Nucleoplasmin_core_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR22747 PTHR22747, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF16276 NPM1-C, 1 hit
PF03066 Nucleoplasmin, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF69203 SSF69203, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RI98E5RI98_HUMAN
Nucleophosmin
NPM1
111Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E5RGW4E5RGW4_HUMAN
Nucleophosmin
NPM1
59Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS43399.1 [P06748-3]
CCDS4376.1 [P06748-1]
CCDS4377.1 [P06748-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A33423 A32915
I38491

NCBI Reference Sequences

More...
RefSeqi
NP_001032827.1, NM_001037738.2 [P06748-3]
NP_002511.1, NM_002520.6 [P06748-1]
NP_954654.1, NM_199185.3 [P06748-2]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.557550

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000296930; ENSP00000296930; ENSG00000181163 [P06748-1]
ENST00000351986; ENSP00000341168; ENSG00000181163 [P06748-2]
ENST00000393820; ENSP00000377408; ENSG00000181163 [P06748-3]
ENST00000517671; ENSP00000428755; ENSG00000181163 [P06748-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
4869

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4869

UCSC genome browser

More...
UCSCi
uc003mbh.4 human [P06748-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
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[»]
5EHDX-ray2.55A/B/C/D/E/F/G/H/I/J/a/b/c/d/e/f/g/h/i/j9-124[»]
ProteinModelPortaliP06748
SMRiP06748
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110929, 597 interactors
CORUMiP06748
DIPiDIP-30932N
IntActiP06748, 275 interactors
MINTiP06748
STRINGi9606.ENSP00000296930

Chemistry databases

BindingDBiP06748
ChEMBLiCHEMBL5178

PTM databases

iPTMnetiP06748
PhosphoSitePlusiP06748
SwissPalmiP06748

Polymorphism and mutation databases

BioMutaiNPM1
DMDMi114762

2D gel databases

DOSAC-COBS-2DPAGEiP06748
REPRODUCTION-2DPAGEiIPI00549248
SWISS-2DPAGEiP06748

Proteomic databases

EPDiP06748
MaxQBiP06748
PaxDbiP06748
PeptideAtlasiP06748
PRIDEiP06748
ProteomicsDBi51927
51928 [P06748-2]
51929 [P06748-3]
TopDownProteomicsiP06748-1 [P06748-1]
P06748-2 [P06748-2]
P06748-3 [P06748-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
4869
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

Comparative Toxicogenomics Database

More...
CTDi
4869
DisGeNETi4869
EuPathDBiHostDB:ENSG00000181163.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
NPM1
HGNCiHGNC:7910 NPM1
HPAiCAB012983
HPA011384
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
98842 Lymphomatoid papulosis
300865 Primary cutaneous anaplastic large cell lymphoma
PharmGKBiPA31712

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IHZM Eukaryota
ENOG4111IKX LUCA
GeneTreeiENSGT00940000153052
HOGENOMiHOG000013061
HOVERGENiHBG001860
InParanoidiP06748
KOiK11276
OMAiVEACICS
OrthoDBiEOG091G0NLY
PhylomeDBiP06748
TreeFamiTF327704

Enzyme and pathway databases

ReactomeiR-HSA-180746 Nuclear import of Rev protein
R-HSA-3899300 SUMOylation of transcription cofactors
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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
NPM1 human
EvolutionaryTraceiP06748

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
NPM1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
4869
PMAP-CutDBiP06748

Protein Ontology

More...
PROi
PR:P06748

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000181163 Expressed in 215 organ(s), highest expression level in kidney
ExpressionAtlasiP06748 baseline and differential
GenevisibleiP06748 HS

Family and domain databases

Gene3Di1.10.10.2100, 1 hit
InterProiView protein in InterPro
IPR032569 NPM1_C
IPR038101 NPM1_C_sf
IPR004301 Nucleoplasmin
IPR024057 Nucleoplasmin_core_dom
IPR036824 Nucleoplasmin_core_dom_sf
PANTHERiPTHR22747 PTHR22747, 1 hit
PfamiView protein in Pfam
PF16276 NPM1-C, 1 hit
PF03066 Nucleoplasmin, 1 hit
SUPFAMiSSF69203 SSF69203, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiNPM_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>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
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: December 5, 2018
This is version 230 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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