CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004092
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
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
27GCELKADKDYHFKVDacetylation[1]
32ADKDYHFKVDNDENEacetylation[1]
54VSLGAGAKDELHIVEacetylation[1]
150SAPGGGNKVPQKKVKacetylation[1]
154GGNKVPQKKVKLDEDacetylation[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
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV 60
EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE 120
EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDDEDDEDDE DDEDDDDDDF 180
DEEETEEKVP VKKSVRDTPA KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS 240
SVEDIKAKMQ ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL 292 
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