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Q80W85 (NPM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleoplasmin-2
Gene names
Name:Npm2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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 By similarity.

Subcellular location

Nucleus. Note: Found in the oocyte nucleus before nuclear membrane breakdown, after which it is redistributed to the cytoplasm. Ref.1

Tissue specificity

Ovary specific. Ref.1

Domain

The acidic tract A2 mediates histone binding By similarity.

Sequence similarities

Belongs to the nucleoplasmin family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Nucleoplasmin-2
PRO_0000219488

Regions

Region129 – 15224Acidic tract A2 By similarity
Motif165 – 18016Bipartite nuclear localization signal By similarity
Compositional bias128 – 14114Poly-Glu
Compositional bias168 – 1714Poly-Lys

Sites

Site571Interaction between pentamers By similarity
Site841Interaction between pentamers By similarity

Experimental info

Sequence conflict1961S → F in BAC35815. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q80W85 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8B8A8931F85032EE

FASTA20723,309
        10         20         30         40         50         60 
MSRHSTSSVT ETTAKNMLWG SELNQEKQTC TFRGQGEKKD SCKLLLSTIC LGEKAKEEVN 

        70         80         90        100        110        120 
RVEVLSQEGR KPPITIATLK ASVLPMVTVS GIELSPPVTF RLRTGSGPVF LSGLECYETS 

       130        140        150        160        170        180 
DLTWEDDEEE EEEEEEEDED EDADISLEEI PVKQVKRVAP QKQMSIAKKK KVEKEEDETV 

       190        200 
VRPSPQDKSP WKKEKSTPRA KKPVTKK 

« Hide

References

« Hide '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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: 129S6/SvEv.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY262112 mRNA. Translation: AAP33133.1.
AK054533 mRNA. Translation: BAC35815.1.
CCDSCCDS27261.1.
RefSeqNP_851990.2. NM_181345.3.
XP_006519206.1. XM_006519143.1.
XP_006519207.1. XM_006519144.1.
XP_006519208.1. XM_006519145.1.
XP_006519209.1. XM_006519146.1.
XP_006519210.1. XM_006519147.1.
UniGeneMm.347749.

3D structure databases

ProteinModelPortalQ80W85.
SMRQ80W85. Positions 17-117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid236605. 1 interaction.

PTM databases

PhosphoSiteQ80W85.

2D gel databases

REPRODUCTION-2DPAGEQ80W85.

Proteomic databases

PRIDEQ80W85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062629; ENSMUSP00000057365; ENSMUSG00000047911.
GeneID328440.
KEGGmmu:328440.
UCSCuc007uot.2. mouse.

Organism-specific databases

CTD10361.
MGIMGI:1890811. Npm2.

Phylogenomic databases

eggNOGNOG78586.
GeneTreeENSGT00440000034554.
HOGENOMHOG000056457.
HOVERGENHBG045601.
InParanoidQ80W85.
KOK11277.
OMASTICLGE.
OrthoDBEOG7ZWD4F.
PhylomeDBQ80W85.
TreeFamTF327704.

Gene expression databases

BgeeQ80W85.
CleanExMM_NPM2.
GenevestigatorQ80W85.

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

NextBio398309.
PROQ80W85.
SOURCESearch...

Entry information

Entry nameNPM2_MOUSE
AccessionPrimary (citable) accession number: Q80W85
Secondary accession number(s): Q8BW23
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot