UniProt Accession

 NPM_RAT; P13084; Q63698; Q64269 

Genbank Protein ID

 J03969; M37039; M37035; M37036; M37037; M37038; M37041; M37035; M37036; M37037; M37038; M37040; M25062; J04943; J04944; BC060579; BC088088 

Genbank Nucleotide ID

 AAA40796.1; AAA41730.1; AAA41730.1; AAA41730.1; AAA41730.1; AAA41730.1; AAA41731.1; AAA41731.1; AAA41731.1; AAA41731.1; AAA41731.1; AAA41731.1; AAA40795.1; AAA40794.1; AAA40793.1; AAH60579.1; AAH88088.1 

Protein Name

 Nucleophosmin 

Protein Synonyms/Alias

 NPM; Nucleolar phosphoprotein B23; Nucleolar protein NO38; Numatrin 

Gene Name

 Npm1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Rattus norvegicus (Rat) 

NCBI Taxa ID

 10116 

Lysine Modification

Position	Peptide	Type	References
255	KMQASIEKAH*****	acetylation	[1]

Reference

 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 

Functional Description

 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. 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 (By similarity). Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. 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). 

Sequence Annotation

 REGION 1 185 Required for interaction with SENP3 (By
 REGION 1 117 Necessary for interaction with APEX1 (By
 REGION 241 292 Required for nucleolar localization (By
 MOTIF 152 157 Nuclear localization signal (Potential).
 MOTIF 190 196 Nuclear localization signal (Potential).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 4 4 Phosphoserine; by PLK1 and PLK2 (By
 MOD_RES 10 10 Phosphoserine (By similarity).
 MOD_RES 32 32 N6-acetyllysine (By similarity).
 MOD_RES 70 70 Phosphoserine (By similarity).
 MOD_RES 75 75 Phosphothreonine (By similarity).
 MOD_RES 95 95 Phosphothreonine (By similarity).
 MOD_RES 125 125 Phosphoserine; by CDK2.
 MOD_RES 139 139 Phosphoserine (By similarity).
 MOD_RES 150 150 N6-acetyllysine (By similarity).
 MOD_RES 154 154 N6-acetyllysine (By similarity).
 MOD_RES 198 198 Phosphothreonine; by CDK1 and CDK2 (By
 MOD_RES 211 211 N6-acetyllysine (By similarity).
 MOD_RES 217 217 Phosphothreonine; by CDK1 (By
 MOD_RES 225 225 Phosphoserine (By similarity).
 MOD_RES 227 227 N6-acetyllysine (By similarity).
 MOD_RES 228 228 N6-acetyllysine; alternate (By
 MOD_RES 232 232 Phosphothreonine; by CDK1 (By
 MOD_RES 235 235 Phosphothreonine; by CDK1 (By
 MOD_RES 240 240 Phosphoserine (By similarity).
 MOD_RES 241 241 Phosphoserine (By similarity).
 MOD_RES 248 248 N6-acetyllysine (By similarity).
 MOD_RES 252 252 Phosphoserine (By similarity).
 MOD_RES 255 255 N6-acetyllysine (By similarity).
 MOD_RES 258 258 Phosphoserine (By similarity).
 MOD_RES 265 265 N6-acetyllysine (By similarity).
 MOD_RES 271 271 N6-acetyllysine (By similarity).
 MOD_RES 277 277 Phosphothreonine (By similarity).
 MOD_RES 290 290 N6-acetyllysine (By similarity).
 CROSSLNK 228 228 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 261 261 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 Acetylation; ADP-ribosylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 292 AA 

Protein Sequence

Gene Ontology

 GO:0005813; C:centrosome; ISS:UniProtKB.
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005730; C:nucleolus; IDA:RGD.
 GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
 GO:0003677; F:DNA binding; IDA:RGD.
 GO:0019899; F:enzyme binding; IDA:RGD.
 GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
 GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IPI:RGD.
 GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
 GO:0007569; P:cell aging; ISS:UniProtKB.
 GO:0007098; P:centrosome cycle; ISS:UniProtKB.
 GO:0006281; P:DNA repair; ISS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
 GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; ISS:UniProtKB.
 GO:0043085; P:positive regulation of catalytic activity; IDA:RGD.
 GO:0045740; P:positive regulation of DNA replication; IDA:RGD.
 GO:0045727; P:positive regulation of translation; ISS:UniProtKB.
 GO:0051260; P:protein homooligomerization; IDA:RGD.
 GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
 GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; ISS:UniProtKB.
 GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
 GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB.
 GO:0043523; P:regulation of neuron apoptotic process; IMP:RGD. 

Interpro

 IPR004301; Nucleoplasmin.
 IPR024057; Nucleoplasmin_core_dom. 

Pfam

  

SMART

  

PROSITE

  

PRINTS