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P06748 (NPM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleophosmin

Short name=NPM
Alternative name(s):
Nucleolar phosphoprotein B23
Nucleolar protein NO38
Numatrin
Gene names
Name:NPM1
Synonyms:NPM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Negatively regulates the activation of EIF2AK2/PKR and suppresses apoptosis through inhibition of EIF2AK2/PKR autophosphorylation. Ref.21 Ref.34 Ref.38 Ref.46 Ref.50 Ref.55 Ref.59 Ref.60

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 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. Ref.20 Ref.21 Ref.27 Ref.31 Ref.33 Ref.38 Ref.40 Ref.41 Ref.42 Ref.50 Ref.54 Ref.59 Ref.60

Subcellular location

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. Ref.6 Ref.29 Ref.31 Ref.42 Ref.50 Ref.54 Ref.60

Post-translational modification

Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. Ref.17 Ref.34

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. Ref.17 Ref.21 Ref.26 Ref.31 Ref.32 Ref.55 Ref.56

Sumoylated by ARF. Ref.35

Involvement in disease

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.

Sequence similarities

Belongs to the nucleoplasmin family.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseProto-oncogene
   LigandRNA-binding
   Molecular functionChaperone
   PTMAcetylation
ADP-ribosylation
Disulfide bond
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCENP-A containing nucleosome assembly at centromere

Traceable author statement. Source: Reactome

DNA repair

Inferred from direct assay Ref.50. Source: UniProtKB

cell aging

Inferred from mutant phenotype PubMed 12080348. Source: UniProtKB

centrosome cycle

Inferred from mutant phenotype Ref.26. Source: UniProtKB

intracellular protein transport

Traceable author statement PubMed 12080348. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay Ref.21. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 12080348. Source: UniProtKB

negative regulation of centrosome duplication

Inferred from mutant phenotype PubMed 16041368. Source: UniProtKB

negative regulation of protein kinase activity by regulation of protein phosphorylation

Inferred from direct assay Ref.21. Source: UniProtKB

nucleocytoplasmic transport

Inferred from direct assay PubMed 16041368. Source: UniProtKB

nucleosome assembly

Inferred from direct assay PubMed 11602260. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 15087454. Source: UniProtKB

positive regulation of translation

Inferred from direct assay Ref.21. Source: UniProtKB

protein localization

Inferred from direct assay PubMed 18420587. Source: UniProtKB

protein oligomerization

Inferred from direct assay Ref.46. Source: MGI

regulation of centriole replication

Inferred from mutant phenotype Ref.55. Source: UniProtKB

regulation of eIF2 alpha phosphorylation by dsRNA

Inferred from direct assay Ref.21. Source: UniProtKB

regulation of endodeoxyribonuclease activity

Inferred from direct assay Ref.50. Source: UniProtKB

regulation of endoribonuclease activity

Inferred from direct assay Ref.50. Source: UniProtKB

response to stress

Inferred from mutant phenotype PubMed 12080348. Source: UniProtKB

ribosome assembly

Traceable author statement PubMed 12080348. Source: UniProtKB

signal transduction

Non-traceable author statement PubMed 16130169. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcentrosome

Inferred from direct assay Ref.26. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 9121481. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleolus

Inferred from direct assay PubMed 12080348PubMed 16041368PubMed 17475909Ref.50. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.28. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12080348. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.46. Source: MGI

spindle pole centrosome

Inferred from direct assay PubMed 16041368. Source: UniProtKB

   Molecular_functionNF-kappaB binding

Inferred from direct assay PubMed 15087454. Source: UniProtKB

RNA binding

Inferred from direct assay Ref.28. Source: UniProtKB

Tat protein binding

Inferred from direct assay PubMed 9094689. Source: UniProtKB

histone binding

Inferred from direct assay PubMed 11602260. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein heterodimerization activity

Inferred from mutant phenotype PubMed 12080348. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 9121481. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.55. Source: UniProtKB

protein kinase inhibitor activity

Inferred from direct assay Ref.21. Source: UniProtKB

ribosomal large subunit binding

Inferred from direct assay Ref.46. Source: MGI

ribosomal small subunit binding

Inferred from direct assay Ref.46. Source: MGI

transcription coactivator activity

Inferred from direct assay PubMed 15087454. Source: UniProtKB

unfolded protein binding

Inferred from direct assay PubMed 10211837. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06748-1)

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.
Isoform 2 (identifier: P06748-2)

The sequence of this isoform differs from the canonical sequence as follows:
     195-223: Missing.
Isoform 3 (identifier: P06748-3)

The sequence of this isoform differs from the canonical sequence as follows:
     258-294: GGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL → AH
Note: Contains a N6-acetyllysine at position 257. Contains a phosphoserine at position 254.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Nucleophosmin
PRO_0000219481

Regions

Region1 – 186186Required for interaction with SENP3
Region1 – 117117Necessary for interaction with APEX1
Region243 – 29452Required for nucleolar localization
Motif152 – 1576Nuclear localization signal Potential
Motif191 – 1977Nuclear localization signal Potential
Compositional bias1 – 99Met-rich
Compositional bias120 – 13213Asp/Glu-rich (acidic)
Compositional bias161 – 18828Asp/Glu-rich (highly acidic)

Sites

Site551Interaction between pentamers By similarity
Site801Interaction between pentamers By similarity
Site175 – 1762Breakpoint for translocation to form NPM1-MLF1

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17 Ref.49 Ref.57 Ref.61 Ref.62
Modified residue41Phosphoserine; by PLK1 and PLK2 Ref.32 Ref.55 Ref.57 Ref.61
Modified residue101Phosphoserine Ref.57
Modified residue321N6-acetyllysine Ref.53
Modified residue701Phosphoserine Ref.36 Ref.39 Ref.44 Ref.45 Ref.47 Ref.52 Ref.57 Ref.61
Modified residue751Phosphothreonine Ref.47
Modified residue951Phosphothreonine Ref.36 Ref.47 Ref.57
Modified residue1251Phosphoserine; by CDK2 Ref.17 Ref.44 Ref.45 Ref.47 Ref.48 Ref.51 Ref.52 Ref.57 Ref.61
Modified residue1371Phosphoserine Ref.57
Modified residue1391Phosphoserine Ref.47 Ref.57
Modified residue1501N6-acetyllysine Ref.37 Ref.53
Modified residue1541N6-acetyllysine Ref.37
Modified residue1991Phosphothreonine; by CDK1, CDK2 and CDK6 Ref.39 Ref.56 Ref.57
Modified residue2121N6-acetyllysine Ref.34 Ref.37
Modified residue2191Phosphothreonine; by CDK1
Modified residue2271Phosphoserine Ref.61
Modified residue2291N6-acetyllysine Ref.34
Modified residue2301N6-acetyllysine; alternate Ref.34
Modified residue2341Phosphothreonine; by CDK1 Ref.47
Modified residue2371Phosphothreonine; by CDK1 Ref.47
Modified residue2421Phosphoserine Ref.57
Modified residue2431Phosphoserine Ref.47 Ref.57 Ref.61
Modified residue2501N6-acetyllysine Ref.34
Modified residue2541Phosphoserine Ref.39 Ref.57 Ref.61
Modified residue2571N6-acetyllysine Ref.34 Ref.53
Modified residue2601Phosphoserine Ref.57
Modified residue2671N6-acetyllysine Ref.53
Modified residue2731N6-acetyllysine Ref.53
Modified residue2791Phosphothreonine Ref.44 Ref.57
Modified residue2921N6-acetyllysine Ref.34
Cross-link230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.35
Cross-link263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.35

Natural variations

Alternative sequence195 – 22329Missing in isoform 2.
VSP_003616
Alternative sequence258 – 29437GGSLP…WRKSL → AH in isoform 3.
VSP_043599

Experimental info

Mutagenesis41S → A: Abolishes phosphorylation by PLK2 and impairs centriole duplication. Ref.55
Mutagenesis41S → D or E: Mimicks phosphorylation state, inducing accumulation of centrioles. Ref.55
Mutagenesis951T → A: Does not affect phosphorylation by PLK2. Ref.55
Mutagenesis1251S → A: Does not affect phosphorylation by PLK2. Ref.55
Mutagenesis1991T → A: Partial loss of phosphorylation. Does not affect phosphorylation by PLK2. Ref.28 Ref.55
Mutagenesis2191T → A: Partial loss of phosphorylation. Ref.28
Mutagenesis2341T → A: Partial loss of phosphorylation; when associated with A-237. Ref.28
Mutagenesis2371T → A: Partial loss of phosphorylation. Ref.28
Mutagenesis2481K → A: Partial destabilization of the structure. Ref.64
Mutagenesis2501K → A: Increase in the stabilization of the structure. Ref.64
Mutagenesis2631K → A: Increase in the stabilization of the structure and partial delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-267. Ref.41
Mutagenesis2631K → R: No change in the sumoylation level. Ref.41
Mutagenesis2671K → A: Increase in the stabilization of the structure and complete delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-263.
Mutagenesis2681F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-276. Ref.64
Mutagenesis2761F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-268. Ref.64
Mutagenesis2881W → A: Complete destabilization of the structure; when associated with A-290. Ref.64
Mutagenesis2901W → A: Partial destabilization of the structure. Complete destabilization of the structure; when associated with A-288. Ref.64
Sequence conflict801K → E in AAH21983. Ref.13
Sequence conflict1291E → D AA sequence Ref.22
Sequence conflict1681Missing in AAW67758. Ref.6
Sequence conflict1781D → G in AAH16768. Ref.13
Sequence conflict1831D → N in BAG70175. Ref.11
Sequence conflict1831D → N in BAG70050. Ref.11
Sequence conflict2131D → P in AAA36473. Ref.23
Sequence conflict2131D → P in AAA36474. Ref.23
Sequence conflict2141S → L AA sequence Ref.21
Sequence conflict2161P → S in AAA36473. Ref.23
Sequence conflict219 – 2213TPR → SSS in AAA36473. Ref.23
Sequence conflict2311Q → R in AAQ24860. Ref.8
Sequence conflict2711Y → C in AAH16768. Ref.13
Sequence conflict2871L → F in AAH12566. Ref.13
Sequence conflict288 – 2947WQWRKSL → CLAVEEVSLRK in AAW67752. Ref.6
Sequence conflict288 – 2947WQWRKSL → CLAVEEVSLRK in AAW67755. Ref.6
Sequence conflict288 – 2947WQWRKSL → CMAVEEVSLRK in AAW67753. Ref.6
Sequence conflict288 – 2947WQWRKSL → CMAVEEVSLRK in ABC40399. Ref.7
Sequence conflict288 – 2947WQWRKSL → CVAVEEVSLRK in AAW67754. Ref.6
Sequence conflict290 – 2945WRKSL → SLAQVSLRK in AAW67756. Ref.6
Sequence conflict290 – 2945WRKSL → SLEKVSLRK in AAW67757. Ref.6

Secondary structure

....................... 294
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 620BC7BA2E4A0054

FASTA29432,575
        10         20         30         40         50         60 
MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV 

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

       130        140        150        160        170        180 
EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA DEDDDDDDEE DDDEDDDDDD 

       190        200        210        220        230        240 
FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG 

       250        260        270        280        290 
PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL 

« Hide

Isoform 2 [UniParc].

Checksum: 932BEC3377692D91
Show »

FASTA26529,465
Isoform 3 [UniParc].

Checksum: 6AEAD2909EE0A47A
Show »

FASTA25928,400

References

« Hide 'large scale' references
[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]"Cytoplasmic nucleophosmin in acute myelogenous leukemia with a normal karyotype."
Falini B., Mecucci C., Tiacci E., Alcalay M., Rosati R., Pasqualucci L., La Starza R., Diverio D., Colombo E., Santucci A., Bigerna B., Pacini R., Pucciarini A., Liso A., Vignetti M., Fazi P., Meani N., Pettirossi V. expand/collapse author list , Saglio G., Mandelli F., Lo-Coco F., Pelicci P.-G., Martelli M.F.
N. Engl. J. Med. 352:254-266(2005) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Nucleophosmin/B23 is a target of CDK2/cyclin E in centrosome duplication."
Okuda M., Horn H.F., Tarapore P., Tokuyama Y., Smulian A.G., Chan P.K., Knudsen E.S., Hofmann I.A., Snyder J.D., Bove K.E., Fukasawa K.
Cell 103:127-140(2000) [PubMed] [Europe PMC] [Abstract]
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: MUTAGENESIS OF THR-199; THR-219; THR-234 AND THR-237.
[29]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
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]"Aurora-B regulates RNA methyltransferase NSUN2."
Sakita-Suto S., Kanda A., Suzuki F., Sato S., Takata T., Tatsuka M.
Mol. Biol. Cell 18:1107-1117(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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, 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]"Nucleophosmin phosphorylation by v-cyclin-CDK6 controls KSHV latency."
Sarek G., Jaerviluoma A., Moore H.M., Tojkander S., Vartia S., Biberfeld P., Laiho M., Ojala P.M.
PLoS Pathog. 6:E1000818-E1000818(2010) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23613 mRNA. Translation: AAA36380.1.
M28699 mRNA. Translation: AAA58386.1.
M26697 mRNA. Translation: AAA36385.1.
U89321 expand/collapse EMBL AC list , 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.
PIRA32915. A33423.
I38491.
RefSeqNP_001032827.1. NM_001037738.2.
NP_002511.1. NM_002520.6.
NP_954654.1. NM_199185.3.
UniGeneHs.557550.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LLHNMR-A225-294[»]
2P1BX-ray2.75A/B/C/D/E/F/G/H/I/J9-122[»]
2VXDNMR-A243-294[»]
ProteinModelPortalP06748.
SMRP06748. Positions 15-118, 225-294.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110929. 365 interactions.
DIPDIP-30932N.
IntActP06748. 90 interactions.
MINTMINT-4938330.

Chemistry

BindingDBP06748.
ChEMBLCHEMBL5178.

PTM databases

PhosphoSiteP06748.

Polymorphism databases

DMDM114762.

2D gel databases

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

Proteomic databases

PaxDbP06748.
PRIDEP06748.

Protocols and materials databases

DNASU4869.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296930; ENSP00000296930; ENSG00000181163. [P06748-1]
ENST00000351986; ENSP00000341168; ENSG00000181163. [P06748-2]
ENST00000393820; ENSP00000377408; ENSG00000181163. [P06748-3]
ENST00000517671; ENSP00000428755; ENSG00000181163. [P06748-1]
GeneID4869.
KEGGhsa:4869.
UCSCuc003mbh.3. human. [P06748-3]
uc003mbi.3. human. [P06748-1]
uc003mbj.3. human. [P06748-2]

Organism-specific databases

CTD4869.
GeneCardsGC05P170814.
HGNCHGNC:7910. NPM1.
HPACAB012983.
HPA011384.
HPA053413.
MIM164040. gene.
neXtProtNX_P06748.
Orphanet98834. Acute myeloblastic leukemia with maturation.
98833. Acute myeloblastic leukemia without maturation.
517. Acute myelomonocytic leukemia.
520. Acute promyelocytic leukemia.
PharmGKBPA31712.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG79897.
HOGENOMHOG000013061.
HOVERGENHBG001860.
InParanoidP06748.
KOK11276.
OMANCFRTED.
OrthoDBEOG79W97G.
PhylomeDBP06748.
TreeFamTF327704.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP06748.
BgeeP06748.
GenevestigatorP06748.

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

ChiTaRSNPM1. human.
EvolutionaryTraceP06748.
GeneWikiNPM1.
GenomeRNAi4869.
NextBio18752.
PMAP-CutDBP06748.
PROP06748.
SOURCESearch...

Entry information

Entry nameNPM_HUMAN
AccessionPrimary (citable) accession number: P06748
Secondary accession number(s): A8K3N7 expand/collapse secondary AC list , B5BU00, D3DQL6, P08693, Q12826, Q13440, Q13441, Q14115, Q5EU94, Q5EU95, Q5EU96, Q5EU97, Q5EU98, Q5EU99, Q6V962, Q8WTW5, Q96AT6, Q96DC4, Q96EA5, Q9BYG9, Q9UDJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM