Reviewed, UniProtKB/Swiss-Prot P06748 (NPM_HUMAN)

Names and origin

Protein names

Recommended name:
    Nucleophosmin
      Short name=NPM
Alternative name(s):
    Nucleolar phosphoprotein B23
    Numatrin
    Nucleolar protein NO38

Gene names

Name:	NPM1
Synonyms:	NPM

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	294 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 TP53/p53 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. Ref.29 Ref.46
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.
Subcellular location	Nucleus › nucleolus. Nucleus › nucleoplasm. 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. Ref.5 Ref.25 Ref.39
Post-translational modification	Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. ADP-ribosylated. Phosphorylated at Ser-4 by PLK1. Phosphorylated by CDK2 at Ser-125 and Thr-199. Phosphorylation at Thr-199 may trigger initiation of centrosome duplication. Phosphorylated by CDC2 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 phosphoryled at Ser-70 by NEK2. Ref.15 Ref.22 Ref.27 Ref.28 Ref.31 Ref.33 Ref.34 Ref.36 Ref.37 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Sumoylated by ARF. Ref.30
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	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
Gene Ontology (GO)
Biological process	anti-apoptosis Non-traceable author statement. Source: UniProtKB cell aging Inferred from mutant phenotype. Source: UniProtKB centrosome cycle Ref.22 Inferred from mutant phenotype. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW intracellular protein transport Traceable author statement. Source: UniProtKB negative regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB negative regulation of centrosome duplication Inferred from mutant phenotype. Source: UniProtKB nucleocytoplasmic transport Inferred from direct assay. Source: UniProtKB nucleosome assembly Inferred from direct assay. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from mutant phenotype. Source: UniProtKB protein oligomerization Ref.46 Inferred from direct assay. Source: MGI response to stress Inferred from mutant phenotype. Source: UniProtKB ribosome assembly Traceable author statement. Source: UniProtKB signal transduction Non-traceable author statement. Source: UniProtKB
Cellular component	nucleolus Ref.46 Inferred from direct assay. Source: UniProtKB nucleoplasm Ref.24 Inferred from direct assay. Source: UniProtKB ribonucleoprotein complex Ref.46 Inferred from direct assay. Source: MGI spindle pole centrosome Inferred from direct assay. Source: UniProtKB
Molecular function	NF-kappaB binding Inferred from direct assay. Source: UniProtKB RNA binding Ref.24 Inferred from direct assay. Source: UniProtKB Tat protein binding Inferred from direct assay. Source: UniProtKB histone binding Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Inferred from mutant phenotype. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB ribosomal large subunit binding Ref.46 Inferred from direct assay. Source: MGI ribosomal small subunit binding Ref.46 Inferred from direct assay. Source: MGI transcription coactivator activity Inferred from direct assay. Source: UniProtKB unfolded protein binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q98147	2	EBI-78579,EBI-626601	From a different organism.
LYAR	Q9NX58	1	EBI-78579,EBI-713507
MDM2	Q00987	3	EBI-78579,EBI-389668
PRMT2	P55345	1	EBI-78579,EBI-78458
TP53	P04637	3	EBI-78579,EBI-366083
TP53	P04637	1	EBI-354150,EBI-366083
USF2	Q15853	1	EBI-78579,EBI-1055994

Alternative products

This entry describes 2 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.

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

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

175 – 176

2

Breakpoint for translocation to form NPM1-MLF1

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.15

Modified residue

4

1

Phosphoserine; by PLK1 Ref.27 Ref.31

Modified residue

10

1

Phosphoserine Ref.31 Ref.37

Modified residue

32

1

N6-acetyllysine Ref.48

Modified residue

70

1

Phosphoserine Ref.31 Ref.33 Ref.34 Ref.36 Ref.37 Ref.40 Ref.42 Ref.43

Modified residue

75

1

Phosphothreonine Ref.34 Ref.43

Modified residue

88

1

Phosphoserine Ref.40

Modified residue

95

1

Phosphothreonine Ref.31 Ref.34 Ref.43

Modified residue

106

1

Phosphoserine By similarity

Modified residue

125

1

Phosphoserine; by CDK2 Ref.15 Ref.33 Ref.36 Ref.37 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44

Modified residue

137

1

Phosphoserine Ref.34 Ref.36

Modified residue

139

1

Phosphoserine Ref.43

Modified residue

150

1

N6-acetyllysine Ref.48 Ref.32

Modified residue

154

1

N6-acetyllysine Ref.32

Modified residue

199

1

Phosphothreonine; by CDK2 and CDC2 Ref.28 Ref.31 Ref.34 Ref.36

Modified residue

212

1

N6-acetyllysine Ref.32

Modified residue

219

1

Phosphothreonine; by CDC2

Modified residue

234

1

Phosphothreonine; by CDC2 Ref.36 Ref.43

Modified residue

237

1

Phosphothreonine; by CDC2 Ref.36 Ref.43

Modified residue

243

1

Phosphoserine Ref.37 Ref.43

Modified residue

254

1

Phosphoserine Ref.31 Ref.33 Ref.34 Ref.37 Ref.42 Ref.43

Modified residue

257

1

N6-acetyllysine Ref.48

Modified residue

260

1

Phosphoserine Ref.34 Ref.36 Ref.37 Ref.43

Modified residue

267

1

N6-acetyllysine Ref.48

Modified residue

273

1

N6-acetyllysine Ref.48

Modified residue

279

1

Phosphothreonine Ref.40 Ref.43

Cross-link

230

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.30

Cross-link

263

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.30

Natural variations

Alternative sequence

195 – 223

29

Missing in isoform 2.

VSP_003616

Experimental info

Mutagenesis

199

1

T → A: Partial loss of phosphorylation. Ref.24

Mutagenesis

219

1

T → A: Partial loss of phosphorylation. Ref.24

Mutagenesis

234

1

T → A: Partial loss of phosphorylation; when associated with A-237. Ref.24

Mutagenesis

237

1

T → A: Partial loss of phosphorylation. Ref.24

Mutagenesis

248

1

K → A: Partial destabilization of the structure. Ref.50

Mutagenesis

250

1

K → A: Increase in the stabilization of the structure. Ref.50

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.38

Mutagenesis

263

1

K → R: No change in the sumoylation level. Ref.38

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.50

Mutagenesis

276

1

F → A: Complete destabilization of the structure and loss of nucleolus localization; when associated with A-268. Ref.50

Mutagenesis

288

1

W → A: Complete destabilization of the structure; when associated with A-290. Ref.50

Mutagenesis

290

1

W → A: Partial destabilization of the structure. Complete destabilization of the structure; when associated with A-288. Ref.50

Sequence conflict

80

1

K → E in AAH21983. Ref.11

Sequence conflict

129

1

E → D AA sequence Ref.18

Sequence conflict

168

1

Missing in AAW67758. Ref.5

Sequence conflict

178

1

D → G in AAH16768. Ref.11

Sequence conflict

213

1

D → P in AAA36473. Ref.19

Sequence conflict

213

1

D → P in AAA36474. Ref.19

Sequence conflict

216

1

P → S in AAA36473. Ref.19

Sequence conflict

219 – 221

3

TPR → SSS in AAA36473. Ref.19

Sequence conflict

231

1

Q → R in AAQ24860. Ref.7

Sequence conflict

271

1

Y → C in AAH16768. Ref.11

Sequence conflict

287

1

L → F in AAH12566. Ref.11

Sequence conflict

288 – 294

7

WQWRKSL → CLAVEEVSLRK in AAW67752. Ref.5

Sequence conflict

288 – 294

7

WQWRKSL → CLAVEEVSLRK in AAW67755. Ref.5

Sequence conflict

288 – 294

7

WQWRKSL → CMAVEEVSLRK in AAW67753. Ref.5

Sequence conflict

288 – 294

7

WQWRKSL → CMAVEEVSLRK Ref.6

Sequence conflict

288 – 294

7

WQWRKSL → CVAVEEVSLRK in AAW67754. Ref.5

Sequence conflict

290 – 294

5

WRKSL → SLAQVSLRK in AAW67756. Ref.5

Sequence conflict

290 – 294

5

WRKSL → SLEKVSLRK in AAW67757. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

294

Helix Strand Turn

Details...

Helix

243 – 256

14

Helix

265 – 276

12

Helix

281 – 293

13

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. 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

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: 2713355] [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: 2775293] [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: 2478125] [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: 9092633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]	"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: 15659725] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INVOLVEMENT IN ACUTE MYELOGENOUS LEUKEMIA. Tissue: Bone marrow.
[6]	"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: 16574551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"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.
[8]	"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).
[9]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Embryo.
[10]	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].
[11]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Bone marrow, Brain, Kidney, Lung, Prostate, Testis and Urinary bladder.
[12]	"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: 8562957] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-133, CHROMOSOMAL TRANSLOCATION WITH RARA. Tissue: Bone marrow.
[13]	"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: 8122112] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, CHROMOSOMAL TRANSLOCATION WITH ALK. Tissue: T-cell lymphoma.
[14]	"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: 8633037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-117, CHROMOSOMAL TRANSLOCATION WITH ALK. Tissue: Lymphoma.
[15]	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.
[16]	"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: 2602120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 15-294 (ISOFORM 1). Tissue: Placenta.
[17]	"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: 9150948] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-54. Tissue: Colon carcinoma.
[18]	"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: 3944116] [Abstract] Cited for: PROTEIN SEQUENCE OF 115-134.
[19]	"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: 2429957] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 213-294 (ISOFORM 1), PROTEIN SEQUENCE OF 227-294.
[20]	"Modification of nucleolar protein B23 after exposure to ionizing radiation." Ramsamooj P., Notario V., Dritschilo A. Radiat. Res. 143:158-164(1995) [PubMed: 7631008] [Abstract] Cited for: ADP-RIBOSYLATION.
[21]	"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: 8570204] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH MLF1.
[22]	"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: 11051553] [Abstract] Cited for: PHOSPHORYLATION BY CDK2.
[23]	"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: 11309377] [Abstract] Cited for: INTERACTION WITH HEPATITIS DELTA VIRUS S-HDAG.
[24]	"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: 12058066] [Abstract] Cited for: MUTAGENESIS OF THR-199; THR-219; THR-234 AND THR-237.
[25]	"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: 12429849] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[26]	"The role of nucleophosmin in centrosome duplication." Okuda M. Oncogene 21:6170-6174(2002) [PubMed: 12214246] [Abstract] Cited for: REVIEW.
[27]	"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: 15190079] [Abstract] Cited for: PHOSPHORYLATION AT SER-4 BY PLK1.
[28]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-199, MASS SPECTROMETRY.
[29]	"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: 16107701] [Abstract] Cited for: ACETYLATION, FUNCTION AS A CHAPERONE.
[30]	"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: 15897463] [Abstract] Cited for: SUMOYLATION AT LYS-230 AND LYS-263.
[31]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-10; SER-70; THR-95; THR-199 AND SER-254, MASS SPECTROMETRY. Tissue: Epithelium.
[32]	"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: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-150; LYS-154 AND LYS-212, MASS SPECTROMETRY. Tissue: Epithelium.
[33]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-125 AND SER-254, MASS SPECTROMETRY. Tissue: Epithelium.
[34]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-75; THR-95; SER-137; THR-199; SER-254 AND SER-260, MASS SPECTROMETRY. Tissue: Epithelium.
[35]	"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: 17215513] [Abstract] Cited for: INTERACTION WITH NSUN2.
[36]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-125; SER-137; THR-199; THR-234; THR-237 AND SER-260, MASS SPECTROMETRY.
[37]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-70; SER-125; SER-243; SER-254 AND SER-260, MASS SPECTROMETRY.
[38]	"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: 18259216] [Abstract] Cited for: INTERACTION WITH SENP3, MUTAGENESIS OF LYS-263.
[39]	"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: 19015314] [Abstract] Cited for: INTERACTION WITH SENP3, SUBCELLULAR LOCATION.
[40]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-88; SER-125 AND THR-279, MASS SPECTROMETRY.
[41]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. Tissue: T-cell.
[42]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-125 AND SER-254, MASS SPECTROMETRY.
[43]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; THR-75; THR-95; SER-125; SER-139; THR-234; THR-237; SER-243; SER-254; SER-260 AND THR-279, MASS SPECTROMETRY.
[44]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. Tissue: Liver.
[45]	"The structure and functions of NPM1/Nucleophsmin/B23, a multifunctional nucleolar acidic protein." Okuwaki M. J. Biochem. 143:441-448(2008) [PubMed: 18024471] [Abstract] Cited for: REVIEW.
[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: 18809582] [Abstract] Cited for: FUNCTION.
[47]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[48]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-150; LYS-257; LYS-267 AND LYS-273, MASS SPECTROMETRY.
[49]	"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: 17879352] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 9-124.
[50]	"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: 18511415] [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

EMBLGenBankDDBJ

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.
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.
CH471062 Genomic DNA. Translation: EAW61443.1.
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.
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.

PIR

A32915. A33423.
I38491.

RefSeq

NP_002511.1.
NP_954654.1.

UniGene

Hs.557550
Hs.654469
Hs.654583

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P1B	X-ray	2.75	A/B/C/D/E/F/G/H/I/J	9-122	[»]
2VXD	NMR	-	A	243-294	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P06748. 92 interactions.

STRING

P06748.

PTM databases

PhosphoSite

P06748.

2-D gel databases

SWISS-2DPAGE

P06748.

DOSAC-COBS-2DPAGE

P06748.

REPRODUCTION-2DPAGE

IPI00549248.

Proteomic databases

PRIDE

P06748.

Genome annotation databases

Ensembl

ENST00000296930; ENSP00000296930; ENSG00000181163; Homo sapiens. [Genome view]
ENST00000351986; ENSP00000341168; ENSG00000181163; Homo sapiens. [Genome view]
ENST00000393820; ENSP00000377408; ENSG00000181163; Homo sapiens. [Genome view]

GeneID

4869.

UCSC

uc003mbi.1. human.
uc003mbj.1. human.

Organism-specific databases

CTD

4869.

GeneCards

GC01P027405.
GC05P170746.

H-InvDB

HIX0005411.

HGNC

HGNC:7910. NPM1.

HPA

CAB012983.
HPA011384.

MIM

164040. gene.

Orphanet

520. Leukemia, promyelocytic, acute.

PharmGKB

PA31712.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P06748.

OMA

TXVEEDA.

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_6185. HIV Infection.

Gene expression databases

ArrayExpress

P06748.

Bgee

P06748.

Genevestigator

P06748.

GermOnline

ENSG00000181163. Homo sapiens.

Family and domain databases

InterPro

IPR004301. Nucleoplasmin.
[Graphical view]

PANTHER

PTHR22747. Nucleoplasmin. 1 hit.

Pfam

PF03066. Nucleoplasmin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

18752.

PMAP-CutDB

P06748.

SOURCE

Search...

Entry information

Entry name

NPM_HUMAN

Accession

Primary (citable) accession number: P06748
Secondary accession number(s): A8K3N7 , P08693, Q12826, Q13440, Q13441, Q14115, Q5EU94, Q5EU95, Q5EU96, Q5EU97, Q5EU98, Q5EU99, Q6V962, Q8WTW5, Q96AT6, Q96DC4, Q96EA5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	November 1, 1990
Last modified:	November 3, 2009
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.