P06748 (NPM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleophosmin
Short name=NPM

Alternative name(s):
Nucleolar phosphoprotein B23
Nucleolar protein NO38
Numatrin

Gene names

Name:	NPM1
Synonyms:	NPM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.33 Ref.37 Ref.45 Ref.48 Ref.53 Ref.57 Ref.58
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. Ref.20 Ref.26 Ref.30 Ref.32 Ref.37 Ref.39 Ref.40 Ref.41 Ref.48 Ref.52 Ref.57 Ref.58
Subcellular location	Nucleus › nucleolus. Nucleus › nucleoplasm. Cytoplasm › cytoskeleton › centrosome. 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.28 Ref.30 Ref.41 Ref.48 Ref.52 Ref.58
Post-translational modification	Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. 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.25 Ref.30 Ref.31 Ref.53 Ref.54 Sumoylated by ARF. Ref.34
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 process	Host-virus interaction
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Ligand	RNA-binding
Molecular function	Chaperone
PTM	ADP-ribosylation Acetylation Disulfide bond Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CENP-A containing nucleosome assembly at centromere Traceable author statement. Source: Reactome DNA repair Inferred from direct assay Ref.48. Source: UniProtKB cell aging Inferred from mutant phenotype PubMed 12080348. Source: UniProtKB centrosome cycle Inferred from mutant phenotype Ref.25. Source: UniProtKB intracellular protein transport Traceable author statement PubMed 12080348. Source: UniProtKB negative regulation of apoptotic process Non-traceable author statement PubMed 16130169. 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 nucleocytoplasmic transport Inferred from direct assay PubMed 16041368. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype PubMed 15087454. Source: UniProtKB protein oligomerization Inferred from direct assay Ref.45. Source: MGI regulation of centriole replication Inferred from mutant phenotype Ref.53. Source: UniProtKB regulation of endodeoxyribonuclease activity Inferred from direct assay Ref.48. Source: UniProtKB regulation of endoribonuclease activity Inferred from direct assay Ref.48. Source: UniProtKB ribosome assembly Traceable author statement PubMed 12080348. Source: UniProtKB signal transduction Non-traceable author statement PubMed 16130169. Source: UniProtKB virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 9121481. Source: UniProtKB nucleolus Inferred from direct assay PubMed 12080348PubMed 16041368PubMed 17475909Ref.48. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.27. Source: UniProtKB ribonucleoprotein complex Inferred from direct assay Ref.45. Source: MGI spindle pole centrosome Inferred from direct assay PubMed 16041368. Source: UniProtKB
Molecular_function	NF-kappaB binding Inferred from direct assay PubMed 15087454. Source: UniProtKB RNA binding Inferred from direct assay Ref.27. Source: UniProtKB Tat protein binding Inferred from direct assay PubMed 9094689. Source: UniProtKB histone binding Inferred from direct assay PubMed 11602260. Source: UniProtKB protein heterodimerization activity Inferred from mutant phenotype PubMed 12080348. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 9121481. Source: UniProtKB ribosomal large subunit binding Inferred from direct assay Ref.45. Source: MGI ribosomal small subunit binding Inferred from direct assay Ref.45. 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q98147	2	EBI-78579,EBI-626601	From a different organism.
MDM2	Q00987	3	EBI-78579,EBI-389668
TP53	P04637	3	EBI-354150,EBI-366083

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 294

294

Nucleophosmin

PRO_0000219481

Regions

Region

1 – 186

186

Required for interaction with SENP3

Region

1 – 117

117

Necessary for interaction with APEX1

Region

243 – 294

52

Required for nucleolar localization

Motif

152 – 157

6

Nuclear localization signal Potential

Motif

191 – 197

7

Nuclear localization signal Potential

Compositional bias

1 – 9

9

Met-rich

Compositional bias

120 – 132

13

Asp/Glu-rich (acidic)

Compositional bias

161 – 188

28

Asp/Glu-rich (highly acidic)

Sites

Site

55

1

Interaction between pentamers By similarity

Site

80

1

Interaction between pentamers By similarity

Site

175 – 176

2

Breakpoint for translocation to form NPM1-MLF1

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.17 Ref.55 Ref.59

Modified residue

4

1

Phosphoserine; by PLK1 and PLK2 Ref.31 Ref.53 Ref.55 Ref.59

Modified residue

10

1

Phosphoserine Ref.55

Modified residue

32

1

N6-acetyllysine Ref.51

Modified residue

70

1

Phosphoserine Ref.35 Ref.38 Ref.43 Ref.44 Ref.46 Ref.50 Ref.55 Ref.59

Modified residue

75

1

Phosphothreonine Ref.46

Modified residue

95

1

Phosphothreonine Ref.35 Ref.46 Ref.55

Modified residue

106

1

Phosphoserine By similarity

Modified residue

125

1

Phosphoserine; by CDK2 Ref.17 Ref.43 Ref.44 Ref.46 Ref.47 Ref.49 Ref.50 Ref.55 Ref.59

Modified residue

137

1

Phosphoserine Ref.55

Modified residue

139

1

Phosphoserine Ref.46 Ref.55

Modified residue

150

1

N6-acetyllysine Ref.36 Ref.51

Modified residue

154

1

N6-acetyllysine Ref.36

Modified residue

199

1

Phosphothreonine; by CDK1, CDK2 and CDK6 Ref.38 Ref.54 Ref.55

Modified residue

212

1

N6-acetyllysine Ref.33 Ref.36

Modified residue

219

1

Phosphothreonine; by CDK1

Modified residue

227

1

Phosphoserine Ref.59

Modified residue

229

1

N6-acetyllysine Ref.33

Modified residue

230

1

N6-acetyllysine; alternate Ref.33

Modified residue

234

1

Phosphothreonine; by CDK1 Ref.46

Modified residue

237

1

Phosphothreonine; by CDK1 Ref.46

Modified residue

242

1

Phosphoserine Ref.55

Modified residue

243

1

Phosphoserine Ref.46 Ref.55 Ref.59

Modified residue

250

1

N6-acetyllysine Ref.33

Modified residue

254

1

Phosphoserine Ref.38 Ref.55 Ref.59

Modified residue

257

1

N6-acetyllysine Ref.33 Ref.51

Modified residue

260

1

Phosphoserine Ref.55

Modified residue

267

1

N6-acetyllysine Ref.51

Modified residue

273

1

N6-acetyllysine Ref.51

Modified residue

279

1

Phosphothreonine Ref.43 Ref.55

Modified residue

292

1

N6-acetyllysine Ref.33

Cross-link

230

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.34

Cross-link

263

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.34

Natural variations

Alternative sequence

195 – 223

29

Missing in isoform 2.

VSP_003616

Alternative sequence

258 – 294

37

GGSLP…WRKSL → AH in isoform 3.

VSP_043599

Experimental info

Mutagenesis

4

1

S → A: Abolishes phosphorylation by PLK2 and impairs centriole duplication. Ref.53

Mutagenesis

4

1

S → D or E: Mimicks phosphorylation state, inducing accumulation of centrioles. Ref.53

Mutagenesis

95

1

T → A: Does not affect phosphorylation by PLK2. Ref.53

Mutagenesis

125

1

S → A: Does not affect phosphorylation by PLK2. Ref.53

Mutagenesis

199

1

T → A: Partial loss of phosphorylation. Does not affect phosphorylation by PLK2. Ref.27 Ref.53

Mutagenesis

219

1

T → A: Partial loss of phosphorylation. Ref.27

Mutagenesis

234

1

T → A: Partial loss of phosphorylation; when associated with A-237. Ref.27

Mutagenesis

237

1

T → A: Partial loss of phosphorylation. Ref.27

Mutagenesis

248

1

K → A: Partial destabilization of the structure. Ref.61

Mutagenesis

250

1

K → A: Increase in the stabilization of the structure. Ref.61

Mutagenesis

263

1

K → 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.40

Mutagenesis

263

1

K → R: No change in the sumoylation level. Ref.40

Mutagenesis

267

1

K → A: Increase in the stabilization of the structure and complete delocalization to the nucleoplasm. Complete delocalization to the nucleoplasm; when associated with A-263.

Mutagenesis

268

1

F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-276. Ref.61

Mutagenesis

276

1

F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-268. Ref.61

Mutagenesis

288

1

W → A: Complete destabilization of the structure; when associated with A-290. Ref.61

Mutagenesis

290

1

W → A: Partial destabilization of the structure. Complete destabilization of the structure; when associated with A-288. Ref.61

Sequence conflict

80

1

K → E in AAH21983. Ref.13

Sequence conflict

129

1

E → D AA sequence Ref.21

Sequence conflict

168

1

Missing in AAW67758. Ref.6

Sequence conflict

178

1

D → G in AAH16768. Ref.13

Sequence conflict

183

1

D → N in BAG70175. Ref.11

Sequence conflict

183

1

D → N in BAG70050. Ref.11

Sequence conflict

213

1

D → P in AAA36473. Ref.22

Sequence conflict

213

1

D → P in AAA36474. Ref.22

Sequence conflict

216

1

P → S in AAA36473. Ref.22

Sequence conflict

219 – 221

3

TPR → SSS in AAA36473. Ref.22

Sequence conflict

231

1

Q → R in AAQ24860. Ref.8

Sequence conflict

271

1

Y → C in AAH16768. Ref.13

Sequence conflict

287

1

L → F in AAH12566. Ref.13

Sequence conflict

288 – 294

7

WQWRKSL → CLAVEEVSLRK in AAW67752. Ref.6

Sequence conflict

288 – 294

7

WQWRKSL → CLAVEEVSLRK in AAW67755. Ref.6

Sequence conflict

288 – 294

7

WQWRKSL → CMAVEEVSLRK in AAW67753. Ref.6

Sequence conflict

288 – 294

7

WQWRKSL → CMAVEEVSLRK in ABC40399. Ref.7

Sequence conflict

288 – 294

7

WQWRKSL → CVAVEEVSLRK in AAW67754. Ref.6

Sequence conflict

290 – 294

5

WRKSL → SLAQVSLRK in AAW67756. Ref.6

Sequence conflict

290 – 294

5

WRKSL → SLEKVSLRK in AAW67757. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

294

Helix Strand Turn

Details...

Beta strand

16 – 19

4

Beta strand

29 – 31

3

Beta strand

41 – 49

9

Beta strand

58 – 65

8

Beta strand

69 – 80

12

Turn

81 – 83

3

Beta strand

84 – 94

11

Beta strand

96 – 105

10

Beta strand

109 – 116

8

Helix

244 – 257

14

Helix

265 – 275

11

Helix

281 – 292

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: 620BC7BA2E4A0054	FASTA	294	32,575
	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
	Isoform 2 [UniParc]. Checksum: 932BEC3377692D91	FASTA	265	29,465
	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 PVKKGQESFK KQEKTPKTPK GPSSVEDIKA KMQASIEKGG SLPKVEAKFI 250 260 NYVKNCFRMT DQEAIQDLWQ WRKSL
	Isoform 3 [UniParc]. Checksum: 6AEAD2909EE0A47A	FASTA	259	28,400
	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 PSSVEDIKAK MQASIEKAH

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	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. , 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, 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]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[29]	"The role of nucleophosmin in centrosome duplication." Okuda M. Oncogene 21:6170-6174(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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.
[35]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[36]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"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.
[38]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[39]	"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.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[44]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[45]	"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.
[46]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[47]	"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, MASS SPECTROMETRY. Tissue: Liver.
[48]	"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, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[49]	"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, MASS SPECTROMETRY.
[50]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[51]	"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, MASS SPECTROMETRY.
[52]	"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.
[53]	"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.
[54]	"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.
[55]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[56]	"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].
[57]	"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.
[58]	"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.
[59]	"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, MASS SPECTROMETRY.
[60]	"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.
[61]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00220740.
IPI00549248.
IPI00658013.

PIR

A32915. A33423.
I38491.

RefSeq

NP_001032827.1. NM_001037738.2.
NP_002511.1. NM_002520.6.
NP_954654.1. NM_199185.3.

UniGene

Hs.557550.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P06748.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-30932N.

IntAct

P06748. 53 interactions.

MINT

MINT-4999760.

PTM databases

PhosphoSite

P06748.

Polymorphism databases

DMDM

114762.

2D gel databases

DOSAC-COBS-2DPAGE

P06748.

REPRODUCTION-2DPAGE

IPI00549248.

SWISS-2DPAGE

P06748.

Proteomic databases

PaxDb

P06748.

PRIDE

P06748.

Protocols and materials databases

DNASU

4869.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296930; ENSP00000296930; ENSG00000181163.
ENST00000351986; ENSP00000341168; ENSG00000181163.
ENST00000393820; ENSP00000377408; ENSG00000181163.
ENST00000517671; ENSP00000428755; ENSG00000181163.

GeneID

4869.

KEGG

hsa:4869.

UCSC

uc003mbi.3. human.
uc003mbj.3. human.

Organism-specific databases

CTD

4869.

GeneCards

GC05P170814.

HGNC

HGNC:7910. NPM1.

HPA

CAB012983.
HPA011384.

MIM

164040. gene.

neXtProt

NX_P06748.

Orphanet

520. Acute promyelocytic leukemia.

PharmGKB

PA31712.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG79897.

HOGENOM

HOG000013061.

HOVERGEN

HBG001860.

InParanoid

P06748.

KO

K11276.

OMA

NCFRTED.

OrthoDB

EOG4W3SNZ.

Enzyme and pathway databases

Pathway_Interaction_DB

aurora_b_pathway. Aurora B signaling.
bard1pathway. BARD1 signaling events.
hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_115566. Cell Cycle.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

P06748.

Bgee

P06748.

Genevestigator

P06748.

GermOnline

ENSG00000181163. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.340. 1 hit.

InterPro

IPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]

PANTHER

PTHR22747. PTHR22747. 1 hit.

SUPFAM

SSF69203. Nucleoplasmin. 1 hit.

ProtoNet

Search...

Other

BindingDB

P06748.

ChEMBL

CHEMBL5178.

ChiTaRS

NPM1. human.

EvolutionaryTrace

P06748.

GenomeRNAi

4869.

NextBio

18752.

PMAP-CutDB

P06748.

SOURCE

Search...

Entry information

Entry name

NPM_HUMAN

Accession

Primary (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 history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 168 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.