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Protein

Nucleophosmin

Gene

NPM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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. In complex with MYC enhances the transcription of MYC target genes.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleophosmin
Short name:
NPM
Gene namesi
Name:NPM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002535981 – 294NucleophosminAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei4Phosphoserine; by PLK1 and PLK2By similarity1
Modified residuei10PhosphoserineBy similarity1
Modified residuei32N6-acetyllysine; alternateBy similarity1
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei43PhosphoserineBy similarity1
Modified residuei67PhosphotyrosineBy similarity1
Modified residuei70PhosphoserineBy similarity1
Modified residuei75PhosphothreonineBy similarity1
Modified residuei95PhosphothreonineBy similarity1
Modified residuei125Phosphoserine; by CDK2By similarity1
Modified residuei137PhosphoserineBy similarity1
Modified residuei139PhosphoserineBy similarity1
Cross-linki141Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei150N6-acetyllysine; alternateBy similarity1
Cross-linki150Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei154N6-acetyllysineBy similarity1
Modified residuei200Phosphothreonine; by CDK1 and CDK2By similarity1
Modified residuei208ADP-ribosylserineBy similarity1
Modified residuei213N6-acetyllysineBy similarity1
Cross-linki216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei219Phosphothreonine; by CDK1By similarity1
Modified residuei227PhosphoserineBy similarity1
Modified residuei229N6-acetyllysineBy similarity1
Modified residuei230N6-acetyllysine; alternateBy similarity1
Cross-linki230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Modified residuei234PhosphothreonineBy similarity1
Modified residuei237PhosphothreonineBy similarity1
Modified residuei242PhosphoserineBy similarity1
Modified residuei243PhosphoserineBy similarity1
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei250N6-acetyllysine; alternateBy similarity1
Cross-linki250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei254PhosphoserineBy similarity1
Modified residuei257N6-acetyllysine; alternateBy similarity1
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei260PhosphoserineBy similarity1
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei267N6-acetyllysine; alternateBy similarity1
Modified residuei267N6-succinyllysine; alternateBy similarity1
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei273N6-acetyllysine; alternateBy similarity1
Cross-linki273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei279PhosphothreonineBy similarity1
Modified residuei292N6-acetyllysineBy similarity1

Post-translational modificationi

Acetylated at C-terminal lysine residues, thereby increasing affinity to histones.By similarity
ADP-ribosylated.By similarity
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-200. Phosphorylation at Thr-200 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-200, 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-200 phosphorylated form has higher affinity for ROCK2 (By similarity).By similarity
Sumoylated by ARF.By similarity
May be ubiquitinated. Ubiquitination leads to proteasomal degradation.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ3T160.
PeptideAtlasiQ3T160.
PRIDEiQ3T160.

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. 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. Interacts with DDX31; this interaction prevents interaction between NPM1 and HDM2. Interacts with MYC; competitive with NOP53. Interacts with NOP53; the interaction is direct and competitive with MYC. Interacts with LRRC34. Interacts with RRP1B.By similarity

Sites

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020363.

Structurei

3D structure databases

ProteinModelPortaliQ3T160.
SMRiQ3T160.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 187Required for interaction with SENP3By similarityAdd BLAST187
Regioni1 – 117Necessary for interaction with APEX1By similarityAdd BLAST117
Regioni243 – 294Required for nucleolar localizationBy similarityAdd BLAST52

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi152 – 157Nuclear localization signalSequence analysis6
Motifi192 – 198Nuclear localization signalSequence analysis7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 9Met-rich9
Compositional biasi120 – 132Asp/Glu-rich (acidic)Add BLAST13
Compositional biasi163 – 189Asp/Glu-rich (highly acidic)Add BLAST27

Sequence similaritiesi

Belongs to the nucleoplasmin family.Curated

Phylogenomic databases

eggNOGiENOG410IHZM. Eukaryota.
ENOG4111IKX. LUCA.
HOGENOMiHOG000013061.
HOVERGENiHBG001860.
InParanoidiQ3T160.
KOiK11276.

Family and domain databases

InterProiView protein in InterPro
IPR032569. NPM1_C.
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.

Sequencei

Sequence statusi: Complete.

Q3T160-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEDSMDMDMS PLRPQNYLFG CELKADRDYH FKVDNDENEH QLSLRTVSLG
60 70 80 90 100
AGAKDELHVV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL
110 120 130 140 150
RLKCGSGPVH ISGQHLVAVE EDAESEEEEE EEVKLLSISG KRSAPGSGSK
160 170 180 190 200
VPQKKVKLAA DEDEDDDDDD DDDDDEDDDD DDFDEEVEEK APVKKSVRDT
210 220 230 240 250
PAKNAQKSNQ NGKDSKPSTP RSKGQESFKK QEKTPKTPRG PSSVEDIKAK
260 270 280 290
MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL
Length:294
Mass (Da):32,703
Last modified:October 11, 2005 - v1
Checksum:i644EBD839DDF160A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102099 mRNA. Translation: AAI02100.1.
RefSeqiNP_001030518.1. NM_001035441.2.
UniGeneiBt.61659.

Genome annotation databases

GeneIDi614028.
KEGGibta:614028.

Similar proteinsi

Entry informationi

Entry nameiNPM_BOVIN
AccessioniPrimary (citable) accession number: Q3T160
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 11, 2005
Last modified: November 22, 2017
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families