UniProt Accession

 NPM_HUMAN; P06748; A8K3N7; B5BU00; D3DQL6; P08693; Q12826; Q13440; Q13441; Q14115; Q5EU94; Q5EU95; Q5EU96; Q5EU97; Q5EU98; Q5EU99; Q6V962; Q8WTW5; Q96AT6; Q96DC4; Q96EA5; Q9BYG9; Q9UDJ7 

Genbank Protein ID

 M23613; M28699; M26697; U89321; U89309; U89310; U89311; U89313; U89314; U89317; U89319; AB042278; AY740634; AY740635; AY740636; AY740637; AY740638; AY740639; AY740640; DQ303464; AY347529; BT007011; AK290652; AB451236; AB451361; CH471062; CH471062; BC002398; BC008495; BC009623; BC012566; BC014349; BC016716; BC016768; BC016824; BC021668; BC021983; BC050628; BC107754; U41742; U41743; U04946; D45915; X16934; J02590; M31004 

Genbank Nucleotide ID

 AAA36380.1; AAA58386.1; AAA36385.1; AAB94739.1; AAB94739.1; AAB94739.1; AAB94739.1; AAB94739.1; AAB94739.1; AAB94739.1; AAB94739.1; BAB40600.1; AAW67752.1; AAW67753.1; AAW67754.1; AAW67755.1; AAW67756.1; AAW67757.1; AAW67758.1; ABC40399.1; AAQ24860.1; AAP35657.1; BAF83341.1; BAG70050.1; BAG70175.1; EAW61443.1; EAW61446.1; AAH02398.1; AAH08495.1; AAH09623.1; AAH12566.1; AAH14349.1; AAH16716.1; AAH16768.1; AAH16824.1; AAH21668.1; AAH21983.1; AAH50628.1; AAI07755.1; AAB00112.1; AAB00113.1; AAA58698.1; BAA08343.1; CAA34809.1; AAA36473.1; AAA36474.1 

Protein Name

 Nucleophosmin 

Protein Synonyms/Alias

 NPM; Nucleolar phosphoprotein B23; Nucleolar protein NO38; Numatrin 

Gene Name

 NPM1 

Gene Synonyms/Alias

 NPM 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
27	GCELKADKDYHFKVD	ubiquitination	[1]
32	ADKDYHFKVDNDENE	ubiquitination	[1]
54	VSLGAGAKDELHIVE	ubiquitination	[1]
80	KVTLATLKMSVQPTV	ubiquitination	[1]
141	KLLSISGKRSAPGGG	ubiquitination	[1]
157	KVPQKKVKLAADEDD	ubiquitination	[1, 2, 3]
189	DDEEAEEKAPVKKGQ	ubiquitination	[3]
193	AEEKAPVKKGQESFK	ubiquitination	[1, 2, 3]
238	SLPKVEAKFINYVKN	ubiquitination	[1]

Reference

 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

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. 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. 

Sequence Annotation

 REGION 1 186 Required for interaction with SENP3.
 REGION 1 117 Necessary for interaction with APEX1.
 REGION 243 294 Required for nucleolar localization.
 MOTIF 152 157 Nuclear localization signal (Potential).
 MOTIF 191 197 Nuclear localization signal (Potential).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 4 4 Phosphoserine; by PLK1 and PLK2.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 32 32 N6-acetyllysine.
 MOD_RES 70 70 Phosphoserine.
 MOD_RES 75 75 Phosphothreonine.
 MOD_RES 95 95 Phosphothreonine.
 MOD_RES 125 125 Phosphoserine; by CDK2.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 139 139 Phosphoserine.
 MOD_RES 150 150 N6-acetyllysine.
 MOD_RES 154 154 N6-acetyllysine.
 MOD_RES 199 199 Phosphothreonine; by CDK1, CDK2 and CDK6.
 MOD_RES 212 212 N6-acetyllysine.
 MOD_RES 219 219 Phosphothreonine; by CDK1.
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 229 229 N6-acetyllysine.
 MOD_RES 230 230 N6-acetyllysine; alternate.
 MOD_RES 234 234 Phosphothreonine; by CDK1.
 MOD_RES 237 237 Phosphothreonine; by CDK1.
 MOD_RES 242 242 Phosphoserine.
 MOD_RES 243 243 Phosphoserine.
 MOD_RES 250 250 N6-acetyllysine.
 MOD_RES 254 254 Phosphoserine.
 MOD_RES 257 257 N6-acetyllysine.
 MOD_RES 260 260 Phosphoserine.
 MOD_RES 267 267 N6-acetyllysine.
 MOD_RES 273 273 N6-acetyllysine.
 MOD_RES 279 279 Phosphothreonine.
 MOD_RES 292 292 N6-acetyllysine.
 CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 263 263 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; Chaperone; Chromosomal rearrangement; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond; Host-virus interaction; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; RNA-binding; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 294 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
 GO:0031616; C:spindle pole centrosome; IDA:UniProtKB.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0051059; F:NF-kappaB binding; IDA:UniProtKB.
 GO:0046982; F:protein heterodimerization activity; IMP:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0004860; F:protein kinase inhibitor activity; IDA:UniProtKB.
 GO:0043023; F:ribosomal large subunit binding; IDA:MGI.
 GO:0043024; F:ribosomal small subunit binding; IDA:MGI.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0030957; F:Tat protein binding; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
 GO:0007569; P:cell aging; IMP:UniProtKB.
 GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
 GO:0007098; P:centrosome cycle; IMP:UniProtKB.
 GO:0006281; P:DNA repair; IDA:UniProtKB.
 GO:0006886; P:intracellular protein transport; TAS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
 GO:0010826; P:negative regulation of centrosome duplication; IMP:UniProtKB.
 GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
 GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
 GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
 GO:0051259; P:protein oligomerization; IDA:MGI.
 GO:0046599; P:regulation of centriole replication; IMP:UniProtKB.
 GO:0060735; P:regulation of eIF2 alpha phosphorylation by dsRNA; IDA:UniProtKB.
 GO:0032071; P:regulation of endodeoxyribonuclease activity; IDA:UniProtKB.
 GO:0060699; P:regulation of endoribonuclease activity; IDA:UniProtKB.
 GO:0042255; P:ribosome assembly; TAS:UniProtKB.
 GO:0007165; P:signal transduction; NAS:UniProtKB.
 GO:0016032; P:viral reproduction; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR004301; Nucleoplasmin.
 IPR024057; Nucleoplasmin_core_dom. 

Pfam

  

SMART

  

PROSITE

  

PRINTS