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P06748

- NPM_HUMAN

UniProt

P06748 - NPM_HUMAN

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Protein

Nucleophosmin

Gene

NPM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei55 – 551Interaction between pentamersBy similarity
Sitei80 – 801Interaction between pentamersBy similarity
Sitei175 – 1762Breakpoint for translocation to form NPM1-MLF1

GO - Molecular functioni

  1. histone binding Source: UniProtKB
  2. NF-kappaB binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein heterodimerization activity Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. protein kinase binding Source: UniProtKB
  7. protein kinase inhibitor activity Source: UniProtKB
  8. ribosomal large subunit binding Source: MGI
  9. ribosomal small subunit binding Source: MGI
  10. RNA binding Source: UniProtKB
  11. Tat protein binding Source: UniProtKB
  12. transcription coactivator activity Source: UniProtKB
  13. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. cell aging Source: UniProtKB
  2. CENP-A containing nucleosome assembly Source: Reactome
  3. centrosome cycle Source: UniProtKB
  4. DNA repair Source: UniProtKB
  5. intracellular protein transport Source: UniProtKB
  6. negative regulation of apoptotic process Source: UniProtKB
  7. negative regulation of cell proliferation Source: UniProtKB
  8. negative regulation of centrosome duplication Source: UniProtKB
  9. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
  10. nucleocytoplasmic transport Source: UniProtKB
  11. nucleosome assembly Source: UniProtKB
  12. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  13. positive regulation of translation Source: UniProtKB
  14. protein localization Source: UniProtKB
  15. protein oligomerization Source: MGI
  16. regulation of centriole replication Source: UniProtKB
  17. regulation of eIF2 alpha phosphorylation by dsRNA Source: UniProtKB
  18. regulation of endodeoxyribonuclease activity Source: UniProtKB
  19. regulation of endoribonuclease activity Source: UniProtKB
  20. response to stress Source: UniProtKB
  21. ribosome assembly Source: UniProtKB
  22. signal transduction Source: UniProtKB
  23. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_9395. Nuclear import of Rev protein.

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleophosmin
Short name:
NPM
Alternative name(s):
Nucleolar phosphoprotein B23
Nucleolar protein NO38
Numatrin
Gene namesi
Name:NPM1
Synonyms:NPM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:7910. NPM1.

Subcellular locationi

Nucleusnucleolus. Nucleusnucleoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. Has been found in the cytoplasm in patients with primary acute myelogenous leukemia (AML), but not with secondary AML. Can shuttle between cytoplasm and nucleus. Co- localizes with the methylated form of RPS10 in the granular component (GC) region of the nucleolus. Colocalized with nucleolin and APEX1 in nucleoli. Isoform 1 of NEK2 is required for its localization to the centrosome during mitosis.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
  6. nucleolus Source: UniProtKB
  7. nucleoplasm Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. ribonucleoprotein complex Source: MGI
  10. spindle pole centrosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving NPM1 is found in a form of non-Hodgkin lymphoma. Translocation t(2;5)(p23;q35) with ALK. The resulting chimeric NPM1-ALK protein homodimerize and the kinase becomes constitutively activated.
A chromosomal aberration involving NPM1 is found in a form of acute promyelocytic leukemia. Translocation t(5;17)(q32;q11) with RARA.
A chromosomal aberration involving NPM1 is a cause of myelodysplastic syndrome (MDS). Translocation t(3;5)(q25.1;q34) with MLF1.
Defects in NPM1 are associated with acute myelogenous leukemia (AML). Mutations in exon 12 affecting the C-terminus of the protein are associated with an aberrant cytoplasmic location.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41S → A: Abolishes phosphorylation by PLK2 and impairs centriole duplication. 1 Publication
Mutagenesisi4 – 41S → D or E: Mimicks phosphorylation state, inducing accumulation of centrioles. 1 Publication
Mutagenesisi95 – 951T → A: Does not affect phosphorylation by PLK2. 1 Publication
Mutagenesisi125 – 1251S → A: Does not affect phosphorylation by PLK2. 1 Publication
Mutagenesisi199 – 1991T → A: Partial loss of phosphorylation. Does not affect phosphorylation by PLK2. 2 Publications
Mutagenesisi219 – 2191T → A: Partial loss of phosphorylation. 1 Publication
Mutagenesisi234 – 2341T → A: Partial loss of phosphorylation; when associated with A-237. 1 Publication
Mutagenesisi237 – 2371T → A: Partial loss of phosphorylation. 1 Publication
Mutagenesisi248 – 2481K → A: Partial destabilization of the structure. 1 Publication
Mutagenesisi250 – 2501K → A: Increase in the stabilization of the structure. 1 Publication
Mutagenesisi263 – 2631K → A: Increase in the stabilization of the structure and partial delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-267. 1 Publication
Mutagenesisi263 – 2631K → R: No change in the sumoylation level. 1 Publication
Mutagenesisi267 – 2671K → A: Increase in the stabilization of the structure and complete delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-263.
Mutagenesisi268 – 2681F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-276. 1 Publication
Mutagenesisi276 – 2761F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-268. 1 Publication
Mutagenesisi288 – 2881W → A: Complete destabilization of the structure; when associated with A-290. 1 Publication
Mutagenesisi290 – 2901W → A: Partial destabilization of the structure. Complete destabilization of the structure; when associated with A-288. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti98834. Acute myeloblastic leukemia with maturation.
98833. Acute myeloblastic leukemia without maturation.
517. Acute myelomonocytic leukemia.
520. Acute promyelocytic leukemia.
PharmGKBiPA31712.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294NucleophosminPRO_0000219481Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine5 Publications
Modified residuei4 – 41Phosphoserine; by PLK1 and PLK24 Publications
Modified residuei10 – 101Phosphoserine1 Publication
Modified residuei32 – 321N6-acetyllysine1 Publication
Modified residuei70 – 701Phosphoserine8 Publications
Modified residuei75 – 751Phosphothreonine1 Publication
Modified residuei95 – 951Phosphothreonine3 Publications
Modified residuei125 – 1251Phosphoserine; by CDK29 Publications
Modified residuei137 – 1371Phosphoserine1 Publication
Modified residuei139 – 1391Phosphoserine2 Publications
Modified residuei150 – 1501N6-acetyllysine2 Publications
Modified residuei154 – 1541N6-acetyllysine1 Publication
Modified residuei199 – 1991Phosphothreonine; by CDK1, CDK2 and CDK64 Publications
Modified residuei212 – 2121N6-acetyllysine2 Publications
Modified residuei219 – 2191Phosphothreonine; by CDK11 Publication
Modified residuei227 – 2271Phosphoserine1 Publication
Modified residuei229 – 2291N6-acetyllysine1 Publication
Modified residuei230 – 2301N6-acetyllysine; alternate1 Publication
Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Modified residuei234 – 2341Phosphothreonine; by CDK11 Publication
Modified residuei237 – 2371Phosphothreonine; by CDK12 Publications
Modified residuei242 – 2421Phosphoserine1 Publication
Modified residuei243 – 2431Phosphoserine3 Publications
Modified residuei250 – 2501N6-acetyllysine1 Publication
Modified residuei254 – 2541Phosphoserine3 Publications
Modified residuei257 – 2571N6-acetyllysine2 Publications
Modified residuei260 – 2601Phosphoserine1 Publication
Cross-linki263 – 263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei267 – 2671N6-acetyllysine1 Publication
Modified residuei273 – 2731N6-acetyllysine1 Publication
Modified residuei279 – 2791Phosphothreonine2 Publications
Modified residuei292 – 2921N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated at C-terminal lysine residues, thereby increasing affinity to histones.8 Publications
ADP-ribosylated.
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-199. Phosphorylation at Thr-199 may trigger initiation of centrosome duplication. Phosphorylated by CDK1 at Thr-199, 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-199 phosphorylated form has higher affinity for ROCK2. CDK6 triggers Thr-199 phosphorylation when complexed to Kaposi's sarcoma herpesvirus (KSHV) V-cyclin, leading to viral reactivation by reducing viral LANA levels.18 Publications
Sumoylated by ARF.1 Publication

Keywords - PTMi

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

Proteomic databases

MaxQBiP06748.
PaxDbiP06748.
PRIDEiP06748.

2D gel databases

DOSAC-COBS-2DPAGEP06748.
REPRODUCTION-2DPAGEIPI00549248.
SWISS-2DPAGEP06748.

PTM databases

PhosphoSiteiP06748.

Miscellaneous databases

PMAP-CutDBP06748.

Expressioni

Gene expression databases

BgeeiP06748.
ExpressionAtlasiP06748. baseline and differential.
GenevestigatoriP06748.

Organism-specific databases

HPAiCAB012983.
HPA011384.
HPA053413.

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 By similarity. 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.By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q981472EBI-78579,EBI-626601From a different organism.
AURKAO149653EBI-78579,EBI-448680
AURKBQ96GD45EBI-78579,EBI-624291
CDKN2AQ8N7262EBI-78579,EBI-625922
CPSF1Q105702EBI-78579,EBI-347859
EIF2AK2P195253EBI-78579,EBI-640775
FAM129AQ9BZQ87EBI-78579,EBI-6916466
HDAC1Q135472EBI-78579,EBI-301834
HDAC2Q927692EBI-78579,EBI-301821
HEMGNQ9BXL57EBI-78579,EBI-3916399
L2P249384EBI-78579,EBI-7481199From a different organism.
L2P689515EBI-78579,EBI-7481182From a different organism.
MDM2Q009875EBI-78579,EBI-389668
PELP1Q8IZL83EBI-78579,EBI-716449
pre-C/CB1Q2W98EBI-78579,EBI-9081051From a different organism.
SENP3Q9H4L46EBI-78579,EBI-2880236
TFAP2AP055496EBI-78579,EBI-347351
TP53P046376EBI-78579,EBI-366083
YWHAZP631042EBI-78579,EBI-347088

Protein-protein interaction databases

BioGridi110929. 440 interactions.
DIPiDIP-30932N.
IntActiP06748. 92 interactions.
MINTiMINT-4938330.

Structurei

Secondary structure

1
294
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 194
Beta strandi29 – 313
Beta strandi41 – 499
Beta strandi58 – 658
Beta strandi69 – 8012
Turni81 – 833
Beta strandi84 – 9411
Beta strandi96 – 10510
Beta strandi109 – 1168
Helixi244 – 25714
Helixi265 – 27511
Helixi281 – 29212

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLHNMR-A225-294[»]
2P1BX-ray2.75A/B/C/D/E/F/G/H/I/J9-122[»]
2VXDNMR-A243-294[»]
ProteinModelPortaliP06748.
SMRiP06748. Positions 13-120, 225-294.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06748.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 186186Required for interaction with SENP3Add
BLAST
Regioni1 – 117117Necessary for interaction with APEX1Add
BLAST
Regioni243 – 29452Required for nucleolar localizationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi152 – 1576Nuclear localization signalSequence Analysis
Motifi191 – 1977Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 99Met-rich
Compositional biasi120 – 13213Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi161 – 18828Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the nucleoplasmin family.Curated

Phylogenomic databases

eggNOGiNOG79897.
GeneTreeiENSGT00440000034554.
HOGENOMiHOG000013061.
HOVERGENiHBG001860.
InParanoidiP06748.
KOiK11276.
OMAiNCFRTED.
OrthoDBiEOG79W97G.
PhylomeDBiP06748.
TreeFamiTF327704.

Family and domain databases

Gene3Di2.60.120.340. 1 hit.
InterProiIPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERiPTHR22747. PTHR22747. 1 hit.
SUPFAMiSSF69203. SSF69203. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P06748-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG
60 70 80 90 100
AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL
110 120 130 140 150
RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK
160 170 180 190 200
VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP
210 220 230 240 250
AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK
260 270 280 290
MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL
Length:294
Mass (Da):32,575
Last modified:November 1, 1990 - v2
Checksum:i620BC7BA2E4A0054
GO
Isoform 2 (identifier: P06748-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     195-223: Missing.

Show »
Length:265
Mass (Da):29,465
Checksum:i932BEC3377692D91
GO
Isoform 3 (identifier: P06748-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     258-294: GGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL → AH

Note: Contains a N6-acetyllysine at position 257.

Show »
Length:259
Mass (Da):28,400
Checksum:i6AEAD2909EE0A47A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801K → E in AAH21983. (PubMed:15489334)Curated
Sequence conflicti129 – 1291E → D AA sequence (PubMed:3944116)Curated
Sequence conflicti168 – 1681Missing in AAW67758. (PubMed:15659725)Curated
Sequence conflicti178 – 1781D → G in AAH16768. (PubMed:15489334)Curated
Sequence conflicti183 – 1831D → N in BAG70175. (PubMed:19054851)Curated
Sequence conflicti183 – 1831D → N in BAG70050. (PubMed:19054851)Curated
Sequence conflicti213 – 2131D → P in AAA36473. (PubMed:2429957)Curated
Sequence conflicti213 – 2131D → P in AAA36474. (PubMed:2429957)Curated
Sequence conflicti214 – 2141S → L AA sequence (PubMed:12882984)Curated
Sequence conflicti216 – 2161P → S in AAA36473. (PubMed:2429957)Curated
Sequence conflicti219 – 2213TPR → SSS in AAA36473. (PubMed:2429957)Curated
Sequence conflicti231 – 2311Q → R in AAQ24860. 1 PublicationCurated
Sequence conflicti271 – 2711Y → C in AAH16768. (PubMed:15489334)Curated
Sequence conflicti287 – 2871L → F in AAH12566. (PubMed:15489334)Curated
Sequence conflicti288 – 2947WQWRKSL → CLAVEEVSLRK in AAW67752. (PubMed:15659725)Curated
Sequence conflicti288 – 2947WQWRKSL → CLAVEEVSLRK in AAW67755. (PubMed:15659725)Curated
Sequence conflicti288 – 2947WQWRKSL → CMAVEEVSLRK in AAW67753. (PubMed:15659725)Curated
Sequence conflicti288 – 2947WQWRKSL → CMAVEEVSLRK in ABC40399. (PubMed:16574551)Curated
Sequence conflicti288 – 2947WQWRKSL → CVAVEEVSLRK in AAW67754. (PubMed:15659725)Curated
Sequence conflicti290 – 2945WRKSL → SLAQVSLRK in AAW67756. (PubMed:15659725)Curated
Sequence conflicti290 – 2945WRKSL → SLEKVSLRK in AAW67757. (PubMed:15659725)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei195 – 22329Missing in isoform 2. 1 PublicationVSP_003616Add
BLAST
Alternative sequencei258 – 29437GGSLP…WRKSL → AH in isoform 3. 2 PublicationsVSP_043599Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23613 mRNA. Translation: AAA36380.1.
M28699 mRNA. Translation: AAA58386.1.
M26697 mRNA. Translation: AAA36385.1.
U89321
, U89309, U89310, U89311, U89313, U89314, U89317, U89319 Genomic DNA. Translation: AAB94739.1.
AB042278 mRNA. Translation: BAB40600.1.
AY740634 mRNA. Translation: AAW67752.1.
AY740635 mRNA. Translation: AAW67753.1.
AY740636 mRNA. Translation: AAW67754.1.
AY740637 mRNA. Translation: AAW67755.1.
AY740638 mRNA. Translation: AAW67756.1.
AY740639 mRNA. Translation: AAW67757.1.
AY740640 mRNA. Translation: AAW67758.1.
DQ303464 mRNA. Translation: ABC40399.1.
AY347529 mRNA. Translation: AAQ24860.1.
BT007011 mRNA. Translation: AAP35657.1.
AK290652 mRNA. Translation: BAF83341.1.
AB451236 mRNA. Translation: BAG70050.1.
AB451361 mRNA. Translation: BAG70175.1.
CH471062 Genomic DNA. Translation: EAW61443.1.
CH471062 Genomic DNA. Translation: EAW61446.1.
BC002398 mRNA. Translation: AAH02398.1.
BC008495 mRNA. Translation: AAH08495.1.
BC009623 mRNA. Translation: AAH09623.1.
BC012566 mRNA. Translation: AAH12566.1.
BC014349 mRNA. Translation: AAH14349.1.
BC016716 mRNA. Translation: AAH16716.1.
BC016768 mRNA. Translation: AAH16768.1.
BC016824 mRNA. Translation: AAH16824.1.
BC021668 mRNA. Translation: AAH21668.1.
BC021983 mRNA. Translation: AAH21983.1.
BC050628 mRNA. Translation: AAH50628.1.
BC107754 mRNA. Translation: AAI07755.1.
U41742 mRNA. Translation: AAB00112.1. Different termination.
U41743 mRNA. Translation: AAB00113.1. Different termination.
U04946 mRNA. Translation: AAA58698.1. Different termination.
D45915 mRNA. Translation: BAA08343.1. Different termination.
X16934 mRNA. Translation: CAA34809.1.
J02590 mRNA. Translation: AAA36473.1.
M31004 mRNA. Translation: AAA36474.1.
CCDSiCCDS43399.1. [P06748-3]
CCDS4376.1. [P06748-1]
CCDS4377.1. [P06748-2]
PIRiA33423. A32915.
I38491.
RefSeqiNP_001032827.1. NM_001037738.2. [P06748-3]
NP_002511.1. NM_002520.6. [P06748-1]
NP_954654.1. NM_199185.3. [P06748-2]
UniGeneiHs.557550.

Genome annotation databases

EnsembliENST00000296930; ENSP00000296930; ENSG00000181163. [P06748-1]
ENST00000351986; ENSP00000341168; ENSG00000181163. [P06748-2]
ENST00000393820; ENSP00000377408; ENSG00000181163. [P06748-3]
ENST00000517671; ENSP00000428755; ENSG00000181163. [P06748-1]
GeneIDi4869.
KEGGihsa:4869.
UCSCiuc003mbh.3. human. [P06748-3]
uc003mbi.3. human. [P06748-1]
uc003mbj.3. human. [P06748-2]

Polymorphism databases

DMDMi114762.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23613 mRNA. Translation: AAA36380.1 .
M28699 mRNA. Translation: AAA58386.1 .
M26697 mRNA. Translation: AAA36385.1 .
U89321
, U89309 , U89310 , U89311 , U89313 , U89314 , U89317 , U89319 Genomic DNA. Translation: AAB94739.1 .
AB042278 mRNA. Translation: BAB40600.1 .
AY740634 mRNA. Translation: AAW67752.1 .
AY740635 mRNA. Translation: AAW67753.1 .
AY740636 mRNA. Translation: AAW67754.1 .
AY740637 mRNA. Translation: AAW67755.1 .
AY740638 mRNA. Translation: AAW67756.1 .
AY740639 mRNA. Translation: AAW67757.1 .
AY740640 mRNA. Translation: AAW67758.1 .
DQ303464 mRNA. Translation: ABC40399.1 .
AY347529 mRNA. Translation: AAQ24860.1 .
BT007011 mRNA. Translation: AAP35657.1 .
AK290652 mRNA. Translation: BAF83341.1 .
AB451236 mRNA. Translation: BAG70050.1 .
AB451361 mRNA. Translation: BAG70175.1 .
CH471062 Genomic DNA. Translation: EAW61443.1 .
CH471062 Genomic DNA. Translation: EAW61446.1 .
BC002398 mRNA. Translation: AAH02398.1 .
BC008495 mRNA. Translation: AAH08495.1 .
BC009623 mRNA. Translation: AAH09623.1 .
BC012566 mRNA. Translation: AAH12566.1 .
BC014349 mRNA. Translation: AAH14349.1 .
BC016716 mRNA. Translation: AAH16716.1 .
BC016768 mRNA. Translation: AAH16768.1 .
BC016824 mRNA. Translation: AAH16824.1 .
BC021668 mRNA. Translation: AAH21668.1 .
BC021983 mRNA. Translation: AAH21983.1 .
BC050628 mRNA. Translation: AAH50628.1 .
BC107754 mRNA. Translation: AAI07755.1 .
U41742 mRNA. Translation: AAB00112.1 . Different termination.
U41743 mRNA. Translation: AAB00113.1 . Different termination.
U04946 mRNA. Translation: AAA58698.1 . Different termination.
D45915 mRNA. Translation: BAA08343.1 . Different termination.
X16934 mRNA. Translation: CAA34809.1 .
J02590 mRNA. Translation: AAA36473.1 .
M31004 mRNA. Translation: AAA36474.1 .
CCDSi CCDS43399.1. [P06748-3 ]
CCDS4376.1. [P06748-1 ]
CCDS4377.1. [P06748-2 ]
PIRi A33423. A32915.
I38491.
RefSeqi NP_001032827.1. NM_001037738.2. [P06748-3 ]
NP_002511.1. NM_002520.6. [P06748-1 ]
NP_954654.1. NM_199185.3. [P06748-2 ]
UniGenei Hs.557550.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LLH NMR - A 225-294 [» ]
2P1B X-ray 2.75 A/B/C/D/E/F/G/H/I/J 9-122 [» ]
2VXD NMR - A 243-294 [» ]
ProteinModelPortali P06748.
SMRi P06748. Positions 13-120, 225-294.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110929. 440 interactions.
DIPi DIP-30932N.
IntActi P06748. 92 interactions.
MINTi MINT-4938330.

Chemistry

BindingDBi P06748.
ChEMBLi CHEMBL2111387.

PTM databases

PhosphoSitei P06748.

Polymorphism databases

DMDMi 114762.

2D gel databases

DOSAC-COBS-2DPAGE P06748.
REPRODUCTION-2DPAGE IPI00549248.
SWISS-2DPAGE P06748.

Proteomic databases

MaxQBi P06748.
PaxDbi P06748.
PRIDEi P06748.

Protocols and materials databases

DNASUi 4869.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296930 ; ENSP00000296930 ; ENSG00000181163 . [P06748-1 ]
ENST00000351986 ; ENSP00000341168 ; ENSG00000181163 . [P06748-2 ]
ENST00000393820 ; ENSP00000377408 ; ENSG00000181163 . [P06748-3 ]
ENST00000517671 ; ENSP00000428755 ; ENSG00000181163 . [P06748-1 ]
GeneIDi 4869.
KEGGi hsa:4869.
UCSCi uc003mbh.3. human. [P06748-3 ]
uc003mbi.3. human. [P06748-1 ]
uc003mbj.3. human. [P06748-2 ]

Organism-specific databases

CTDi 4869.
GeneCardsi GC05P170814.
HGNCi HGNC:7910. NPM1.
HPAi CAB012983.
HPA011384.
HPA053413.
MIMi 164040. gene.
neXtProti NX_P06748.
Orphaneti 98834. Acute myeloblastic leukemia with maturation.
98833. Acute myeloblastic leukemia without maturation.
517. Acute myelomonocytic leukemia.
520. Acute promyelocytic leukemia.
PharmGKBi PA31712.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG79897.
GeneTreei ENSGT00440000034554.
HOGENOMi HOG000013061.
HOVERGENi HBG001860.
InParanoidi P06748.
KOi K11276.
OMAi NCFRTED.
OrthoDBi EOG79W97G.
PhylomeDBi P06748.
TreeFami TF327704.

Enzyme and pathway databases

Reactomei REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_9395. Nuclear import of Rev protein.

Miscellaneous databases

ChiTaRSi NPM1. human.
EvolutionaryTracei P06748.
GeneWikii NPM1.
GenomeRNAii 4869.
NextBioi 18752.
PMAP-CutDB P06748.
PROi P06748.
SOURCEi Search...

Gene expression databases

Bgeei P06748.
ExpressionAtlasi P06748. baseline and differential.
Genevestigatori P06748.

Family and domain databases

Gene3Di 2.60.120.340. 1 hit.
InterProi IPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view ]
PANTHERi PTHR22747. PTHR22747. 1 hit.
SUPFAMi SSF69203. SSF69203. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth."
    Chan W.-Y., Liu Q.R., Borjigin J., Busch H., Rennert O.M., Tease L.A., Chan P.-K.
    Biochemistry 28:1033-1039(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "The nucleotide sequence of a human cDNA encoding the highly conserved nucleolar phosphoprotein B23."
    Li X., McNeilage L.J., Whittingham S.
    Biochem. Biophys. Res. Commun. 163:72-78(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: B-cell lymphoma.
  3. "Isolation and characterization of a molecular cDNA clone of a human mRNA from interferon-treated cells encoding nucleolar protein B23, numatrin."
    Zhang X.T., Thomis D.C., Samuel C.E.
    Biochem. Biophys. Res. Commun. 164:176-184(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Amnion.
  4. "Isolation and characterization of the human nucleophosmin/B23 (NPM) gene: identification of the YY1 binding site at the 5' enhancer region."
    Chan P.-K., Chan F.Y., Morris S.W., Xie Z.
    Nucleic Acids Res. 25:1225-1232(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  5. "Human homologue of Rat B23.2."
    Okuwaki M., Nagata K.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INVOLVEMENT IN ACUTE MYELOGENOUS LEUKEMIA.
    Tissue: Bone marrow.
  7. "Cytoplasmic nucleophosmin in myeloid sarcoma occurring 20 years after diagnosis of acute myeloid leukaemia."
    Bolli N., Galimberti S., Martelli M.P., Tabarrini A., Roti G., Mecucci C., Martelli M.F., Petrini M., Falini B.
    Lancet Oncol. 7:350-352(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  8. "Cloning of a new transcript of nucleophosmin in testis."
    Lu L., Huang X.Y., Yin L.L., Xu M., Li J.M., Zhou Z.M., Sha J.H.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryo.
  11. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Tissue: Bone marrow, Brain, Kidney, Lung, Prostate, Testis and Urinary bladder.
  14. "The t(5;17) variant of acute promyelocytic leukemia expresses a nucleophosmin-retinoic acid receptor fusion."
    Redner R.L., Rush E.A., Faas S., Rudert W.A., Corey S.J.
    Blood 87:882-886(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-133, CHROMOSOMAL TRANSLOCATION WITH RARA.
    Tissue: Bone marrow.
  15. "Fusion of a kinase gene, ALK, to a nucleolar protein gene, NPM, in non-Hodgkin's lymphoma."
    Morris S.W., Kirstein M.N., Valentine M.B., Dittmer K.G., Shapiro D.N., Saltman D.L., Look A.T.
    Science 263:1281-1284(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, CHROMOSOMAL TRANSLOCATION WITH ALK.
    Tissue: T-cell lymphoma.
  16. "Characterization of the transforming activity of p80, a hyperphosphorylated protein in a Ki-1 lymphoma cell line with chromosomal translocation t(2;5)."
    Fujimoto J., Shiota M., Iwahara T., Seki N., Satoh H., Mori S., Yamamoto T.
    Proc. Natl. Acad. Sci. U.S.A. 93:4181-4186(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, CHROMOSOMAL TRANSLOCATION WITH ALK.
    Tissue: Lymphoma.
  17. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-24; 33-101; 104-141; 240-248 AND 278-291, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  18. "Nucleotide sequence of a cDNA clone representing a third allele of human protein B23."
    Hale T.K., Mansfield B.C.
    Nucleic Acids Res. 17:10112-10112(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-294 (ISOFORM 1).
    Tissue: Placenta.
  19. "A two-dimensional gel database of human colon carcinoma proteins."
    Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
    Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-54.
    Tissue: Colon carcinoma.
  20. "Nucleolar targeting signal of Rex protein of human T-cell leukemia virus type I specifically binds to nucleolar shuttle protein B-23."
    Adachi Y., Copeland T.D., Hatanaka M., Oroszlan S.
    J. Biol. Chem. 268:13930-13934(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-42; 50-67; 137-151; 218-227; 252-266 AND 277-286 (ISOFORM 1), INTERACTION WITH HTLV1 REX PROTEIN.
  21. "Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR."
    Pang Q., Christianson T.A., Koretsky T., Carlson H., David L., Keeble W., Faulkner G.R., Speckhart A., Bagby G.C.
    J. Biol. Chem. 278:41709-41717(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 33-42; 213-221; 251-257 AND 268-274, FUNCTION, INTERACTION WITH EIF2AK2, PHOSPHORYLATION.
  22. "Amino acid sequence of protein B23 phosphorylation site."
    Chan P.-K., Aldrich M.B., Cook R.G., Busch H.
    J. Biol. Chem. 261:1868-1872(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 115-134.
  23. "Amino acid sequence of a specific antigenic peptide of protein B23."
    Chan P.-K., Chan W.-Y., Yung B.Y.M., Cook R.G., Aldrich M.B., Ku D., Goldknopf I.L., Busch H.
    J. Biol. Chem. 261:14335-14341(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 213-294 (ISOFORM 1), PROTEIN SEQUENCE OF 227-294.
  24. "Modification of nucleolar protein B23 after exposure to ionizing radiation."
    Ramsamooj P., Notario V., Dritschilo A.
    Radiat. Res. 143:158-164(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: ADP-RIBOSYLATION.
  25. "The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid leukemia produces a novel fusion gene, NPM-MLF1."
    Yoneda-Kato N., Look A.T., Kirstein M.N., Valentine M.B., Raimondi S.C., Cohen K.J., Carroll A.J., Morris S.W.
    Oncogene 12:265-275(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH MLF1.
  26. Cited for: PHOSPHORYLATION BY CDK2.
  27. "The nucleolar phosphoprotein B23 interacts with hepatitis delta antigens and modulates the hepatitis delta virus RNA replication."
    Huang W.H., Yung B.Y., Syu W.J., Lee Y.H.
    J. Biol. Chem. 276:25166-25175(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HEPATITIS DELTA VIRUS S-HDAG.
  28. "The RNA binding activity of a ribosome biogenesis factor, nucleophosmin/B23, is modulated by phosphorylation with a cell cycle-dependent kinase and by association with its subtype."
    Okuwaki M., Tsujimoto M., Nagata K.
    Mol. Biol. Cell 13:2016-2030(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-199; THR-219 AND THR-237, MUTAGENESIS OF THR-199; THR-219; THR-234 AND THR-237.
  29. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. "The role of nucleophosmin in centrosome duplication."
    Okuda M.
    Oncogene 21:6170-6174(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  31. "Nek2A kinase regulates the localization of numatrin to centrosome in mitosis."
    Yao J., Fu C., Ding X., Guo Z., Zenreski A., Chen Y., Ahmed K., Liao J., Dou Z., Yao X.
    FEBS Lett. 575:112-118(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2.
  32. "B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of polo-like kinase 1."
    Zhang H., Shi X., Paddon H., Hampong M., Dai W., Pelech S.
    J. Biol. Chem. 279:35726-35734(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-4 BY PLK1.
  33. "RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin."
    Shu X., Fry A.M., Tulloch B., Manson F.D., Crabb J.W., Khanna H., Faragher A.J., Lennon A., He S., Trojan P., Giessl A., Wolfrum U., Vervoort R., Swaroop A., Wright A.F.
    Hum. Mol. Genet. 14:1183-1197(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPGR.
  34. "Human histone chaperone nucleophosmin enhances acetylation-dependent chromatin transcription."
    Swaminathan V., Kishore A.H., Febitha K.K., Kundu T.K.
    Mol. Cell. Biol. 25:7534-7545(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-212; LYS-229; LYS-230; LYS-250; LYS-257 AND LYS-292, FUNCTION AS A CHAPERONE.
  35. "Sumoylation induced by the Arf tumor suppressor: a p53-independent function."
    Tago K., Chiocca S., Sherr C.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:7689-7694(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-230 AND LYS-263.
  36. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND THR-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."
    Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.
    Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150; LYS-154 AND LYS-212, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  38. "Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication."
    Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.
    Mol. Cell. Biol. 26:9016-9034(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ROCK2.
  39. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-199 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  40. Cited for: INTERACTION WITH NSUN2.
  41. "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing."
    Haindl M., Harasim T., Eick D., Muller S.
    EMBO Rep. 9:273-279(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SENP3, MUTAGENESIS OF LYS-263.
  42. "Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases."
    Yun C., Wang Y., Mukhopadhyay D., Backlund P., Kolli N., Yergey A., Wilkinson K.D., Dasso M.
    J. Cell Biol. 183:589-595(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SENP3, SUBCELLULAR LOCATION.
  43. "The structure and functions of NPM1/Nucleophosmin/B23, a multifunctional nucleolar acidic protein."
    Okuwaki M.
    J. Biochem. 143:441-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  44. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-125 AND THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  45. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  46. "Nucleophosmin serves as a rate-limiting nuclear export chaperone for the Mammalian ribosome."
    Maggi L.B. Jr., Kuchenruether M., Dadey D.Y., Schwope R.M., Grisendi S., Townsend R.R., Pandolfi P.P., Weber J.D.
    Mol. Cell. Biol. 28:7050-7065(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  47. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-75; THR-95; SER-125; SER-139; THR-234; THR-237 AND SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  48. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  49. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  50. "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
    Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
    Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  51. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  52. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  53. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-150; LYS-257; LYS-267 AND LYS-273, ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  54. "Methylation of ribosomal protein S10 by protein-arginine methyltransferase 5 regulates ribosome biogenesis."
    Ren J., Wang Y., Liang Y., Zhang Y., Bao S., Xu Z.
    J. Biol. Chem. 285:12695-12705(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RPS10.
  55. "Polo-like kinase 2-dependent phosphorylation of NPM/B23 on serine 4 triggers centriole duplication."
    Krause A., Hoffmann I.
    PLoS ONE 5:E9849-E9849(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-4 BY PLK2, MUTAGENESIS OF SER-4; THR-95; SER-125 AND THR-199.
  56. Cited for: PHOSPHORYLATION AT THR-199 BY CDK6.
  57. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-10; SER-70; THR-95; SER-125; SER-137; SER-139; THR-199; SER-242; SER-243; SER-254; SER-260 AND THR-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  58. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  59. "BRCA2 and nucleophosmin coregulate centrosome amplification and form a complex with the Rho effector kinase ROCK2."
    Wang H.F., Takenaka K., Nakanishi A., Miki Y.
    Cancer Res. 71:68-77(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BRCA2.
  60. "New centromeric component CENP-W is an RNA-associated nuclear matrix protein that interacts with nucleophosmin/B23 protein."
    Chun Y., Park B., Koh W., Lee S., Cheon Y., Kim R., Che L., Lee S.
    J. Biol. Chem. 286:42758-42769(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPW.
  61. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-70; SER-125; SER-227; SER-243 AND SER-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  62. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  63. "Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface."
    Lee H.H., Kim H.S., Kang J.Y., Lee B.I., Ha J.Y., Yoon H.J., Lim S.O., Jung G., Suh S.W.
    Proteins 69:672-678(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 9-124.
  64. "Structural consequences of nucleophosmin mutations in acute myeloid leukemia."
    Grummitt C.G., Townsley F.M., Johnson C.M., Warren A.J., Bycroft M.
    J. Biol. Chem. 283:23326-23332(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 243-294, MUTAGENESIS OF LYS-248; LYS-250; PHE-268; PHE-276; TRP-288 AND TRP-290.

Entry informationi

Entry nameiNPM_HUMAN
AccessioniPrimary (citable) accession number: P06748
Secondary accession number(s): A8K3N7
, B5BU00, D3DQL6, P08693, Q12826, Q13440, Q13441, Q14115, Q5EU94, Q5EU95, Q5EU96, Q5EU97, Q5EU98, Q5EU99, Q6V962, Q8WTW5, Q96AT6, Q96DC4, Q96EA5, Q9BYG9, Q9UDJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: October 29, 2014
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3