Q86SE8 (NPM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoplasmin-2

Gene names

Name:

NPM2

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	214 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization. Ref.5
Subunit structure	Homopentamer, when bound to H2A-H2B dimers only. Homodecamer of two stacked pentamers, when bound to H2A-H2B dimers and H3-H4 tetramers simultaneously. Ref.5
Subcellular location	Nucleus By similarity. Note: Found in the oocyte nucleus before nuclear membrane breakdown, after which it is redistributed to the cytoplasm By similarity.
Domain	The acidic tract A2 mediates histone binding. Ref.5
Sequence similarities	Belongs to the nucleoplasmin family.

Ontologies

Keywords
Biological process	Fertilization
Cellular component	Nucleus
Molecular function	Chaperone Chromatin regulator Developmental protein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin remodeling Inferred from direct assay Ref.1. Source: UniProtKB embryo development Inferred from mutant phenotype Ref.1. Source: UniProtKB oocyte differentiation Inferred from expression pattern Ref.1. Source: UniProtKB positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of catalytic activity Inferred from electronic annotation. Source: Compara positive regulation of meiosis Inferred from mutant phenotype Ref.1. Source: UniProtKB protein homooligomerization Inferred from electronic annotation. Source: Compara regulation of exit from mitosis Inferred from mutant phenotype Ref.1. Source: UniProtKB single fertilization Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular_component	cytoplasmic chromatin Inferred from direct assay Ref.1. Source: UniProtKB nuclear chromatin Inferred from direct assay Ref.1. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA
Molecular_function	histone binding Traceable author statement PubMed 12581654. Source: UniProtKB nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 214

214

Nucleoplasmin-2

PRO_0000219487

Regions

Region

129 – 152

24

Acidic tract A2

Motif

165 – 180

16

Bipartite nuclear localization signal By similarity

Compositional bias

129 – 144

16

Poly-Glu

Compositional bias

177 – 180

4

Poly-Lys

Compositional bias

182 – 187

6

Poly-Glu

Sites

Site

57

1

Interaction between pentamers

Site

84

1

Interaction between pentamers

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

.

214

Helix Strand Turn

Details...

Beta strand

16 – 23

8

Beta strand

29 – 32

4

Beta strand

43 – 51

9

Beta strand

60 – 65

6

Beta strand

78 – 84

7

Turn

85 – 87

3

Beta strand

90 – 98

9

Beta strand

100 – 109

10

Beta strand

113 – 120

8

Sequences

	Sequence		Length	Mass (Da)
	Q86SE8 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: EAE3BEF1DC8E1CC1	FASTA	214	24,152
	10 20 30 40 50 60 MNLSSASSTE EKAVTTVLWG CELSQERRTW TFRPQLEGKQ SCRLLLHTIC LGEKAKEEMH 70 80 90 100 110 120 RVEILPPANQ EDKKMQPVTI ASLQASVLPM VSMVGVQLSP PVTFQLRAGS GPVFLSGQER 130 140 150 160 170 180 YEASDLTWEE EEEEEGEEEE EEEEDDEDED ADISLEEQSP VKQVKRLVPQ KQASVAKKKK 190 200 210 LEKEEEEIRA SVRDKSPVKK AKATARAKKP GFKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Roles of NPM2 in chromatin and nucleolar organization in oocytes and embryos." Burns K.H., Viveiros M.M., Ren Y., Wang P., DeMayo F.J., Frail D.E., Eppig J.J., Matzuk M.M. Science 300:633-636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"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]. Tissue: Cerebellum.
[3]	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].
[4]	"New insights into the nucleophosmin/nucleoplasmin family of nuclear chaperones." Frehlick L.J., Eirin-Lopez J.M., Ausio J. Bioessays 29:49-59(2007) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[5]	"Crystal structure and function of human nucleoplasmin (npm2): a histone chaperone in oocytes and embryos." Platonova O., Akey I.V., Head J.F., Akey C.W. Biochemistry 50:8078-8089(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 14-122, FUNCTION, DOMAIN, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY262113 mRNA. Translation: AAP33134.1.
AY262114 mRNA. Translation: AAP33135.1.
AK094267 mRNA. Translation: BAG52852.1.
CH471080 Genomic DNA. Translation: EAW63731.1.
CH471080 Genomic DNA. Translation: EAW63732.1.

IPI

IPI00328389.

RefSeq

NP_877724.1. NM_182795.1.

UniGene

Hs.131055.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3T30	X-ray	1.90	A/B/C/D/E/F/G/H/I/J	14-122	[»]

ProteinModelPortal

Q86SE8.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000289820.

PTM databases

PhosphoSite

Q86SE8.

Polymorphism databases

DMDM

37537936.

Proteomic databases

PRIDE

Q86SE8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000289820; ENSP00000289820; ENSG00000158806.
ENST00000397940; ENSP00000381032; ENSG00000158806.
ENST00000518119; ENSP00000427741; ENSG00000158806.
ENST00000521157; ENSP00000429413; ENSG00000158806.

GeneID

10361.

KEGG

hsa:10361.

UCSC

uc003xac.3. human.

Organism-specific databases

CTD

10361.

GeneCards

GC08P021881.

HGNC

HGNC:7930. NPM2.

HPA

HPA041070.

MIM

608073. gene.

neXtProt

NX_Q86SE8.

PharmGKB

PA31732.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG78586.

HOGENOM

HOG000056457.

HOVERGEN

HBG045601.

InParanoid

Q86SE8.

KO

K11277.

OMA

STICLGE.

OrthoDB

EOG43N7F0.

PhylomeDB

Q86SE8.

Gene expression databases

ArrayExpress

Q86SE8.

Bgee

Q86SE8.

CleanEx

HS_NPM2.

Genevestigator

Q86SE8.

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

ChiTaRS

NPM2. human.

GenomeRNAi

10361.

NextBio

39277.

SOURCE

Search...

Entry information

Entry name

NPM2_HUMAN

Accession

Primary (citable) accession number: Q86SE8
Secondary accession number(s): B3KSU0, D3DSQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 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.