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Q3T160 (NPM_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleophosmin

Short name=NPM
Gene names
Name:NPM1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. Acts as a chaperonin for the core histones H3, H2B and H4. Stimulates APEX1 endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1 endonuclease activity on AP single-stranded RNA. May exert a control of APEX1 endonuclease activity within nucleoli devoted to repair AP on rDNA and the removal of oxidized rRNA molecules. In concert with BRCA2, regulates centrosome duplication. Regulates centriole duplication: phosphorylation by PLK2 is able to trigger centriole replication By similarity. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation By similarity.

Subunit structure

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 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 NEK2. Interacts with ROCK2 and BRCA2 By similarity. Interacts with RPGR By similarity. Interacts with EIF2AK2/PKR By similarity.

Subcellular location

Nucleusnucleolus. Nucleusnucleoplasm By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity. Note: Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Colocalizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. NEK2 is required for its localization to the centrosome during mitosis. Interacts with CENPW By similarity.

Post-translational modification

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.

Sumoylated by ARF By similarity.

Sequence similarities

Belongs to the nucleoplasmin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   LigandRNA-binding
   Molecular functionChaperone
   PTMAcetylation
ADP-ribosylation
Disulfide bond
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of centriole replication

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of eIF2 alpha phosphorylation by dsRNA

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endodeoxyribonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endoribonuclease activity

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase inhibitor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Nucleophosmin
PRO_0000253598

Regions

Region1 – 187187Required for interaction with SENP3 By similarity
Region1 – 117117Necessary for interaction with APEX1 By similarity
Region243 – 29452Required for nucleolar localization By similarity
Motif152 – 1576Nuclear localization signal Potential
Motif192 – 1987Nuclear localization signal Potential
Compositional bias1 – 99Met-rich
Compositional bias120 – 13213Asp/Glu-rich (acidic)
Compositional bias163 – 18927Asp/Glu-rich (highly acidic)

Sites

Site551Interaction between pentamers By similarity
Site801Interaction between pentamers By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue41Phosphoserine; by PLK1 and PLK2 By similarity
Modified residue101Phosphoserine By similarity
Modified residue321N6-acetyllysine By similarity
Modified residue701Phosphoserine By similarity
Modified residue751Phosphothreonine By similarity
Modified residue951Phosphothreonine By similarity
Modified residue1251Phosphoserine; by CDK2 By similarity
Modified residue1371Phosphoserine By similarity
Modified residue1391Phosphoserine By similarity
Modified residue1501N6-acetyllysine By similarity
Modified residue1541N6-acetyllysine By similarity
Modified residue2001Phosphothreonine; by CDK1 and CDK2 By similarity
Modified residue2131N6-acetyllysine By similarity
Modified residue2191Phosphothreonine; by CDK1 By similarity
Modified residue2271Phosphoserine By similarity
Modified residue2291N6-acetyllysine By similarity
Modified residue2301N6-acetyllysine; alternate By similarity
Modified residue2341Phosphothreonine By similarity
Modified residue2371Phosphothreonine By similarity
Modified residue2421Phosphoserine By similarity
Modified residue2431Phosphoserine By similarity
Modified residue2501N6-acetyllysine By similarity
Modified residue2541Phosphoserine By similarity
Modified residue2571N6-acetyllysine By similarity
Modified residue2601Phosphoserine By similarity
Modified residue2671N6-acetyllysine By similarity
Modified residue2731N6-acetyllysine By similarity
Modified residue2791Phosphothreonine By similarity
Modified residue2921N6-acetyllysine By similarity
Cross-link230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3T160 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 644EBD839DDF160A

FASTA29432,703
        10         20         30         40         50         60 
MEDSMDMDMS PLRPQNYLFG CELKADRDYH FKVDNDENEH QLSLRTVSLG AGAKDELHVV 

        70         80         90        100        110        120 
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE 

       130        140        150        160        170        180 
EDAESEEEEE EEVKLLSISG KRSAPGSGSK VPQKKVKLAA DEDEDDDDDD DDDDDEDDDD 

       190        200        210        220        230        240 
DDFDEEVEEK APVKKSVRDT PAKNAQKSNQ NGKDSKPSTP RSKGQESFKK QEKTPKTPRG 

       250        260        270        280        290 
PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC102099 mRNA. Translation: AAI02100.1.
RefSeqNP_001030518.1. NM_001035441.2.
UniGeneBt.61659.

3D structure databases

ProteinModelPortalQ3T160.
SMRQ3T160. Positions 15-118, 243-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000020363.

Proteomic databases

PaxDbQ3T160.
PRIDEQ3T160.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID614028.
KEGGbta:614028.

Organism-specific databases

CTD4869.

Phylogenomic databases

eggNOGNOG79897.
HOGENOMHOG000013061.
HOVERGENHBG001860.
InParanoidQ3T160.
KOK11276.

Family and domain databases

Gene3D2.60.120.340. 1 hit.
InterProIPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERPTHR22747. PTHR22747. 1 hit.
SUPFAMSSF69203. SSF69203. 1 hit.
ProtoNetSearch...

Other

NextBio20898902.

Entry information

Entry nameNPM_BOVIN
AccessionPrimary (citable) accession number: Q3T160
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 11, 2005
Last modified: January 22, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families