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Q86SE8

- NPM2_HUMAN

UniProt

Q86SE8 - NPM2_HUMAN

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Protein

Nucleoplasmin-2

Gene

NPM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei57 – 571Interaction between pentamers
Sitei84 – 841Interaction between pentamers

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. histone binding Source: UniProtKB
  3. nucleic acid binding Source: InterPro

GO - Biological processi

  1. chromatin remodeling Source: UniProtKB
  2. embryo development Source: UniProtKB
  3. oocyte differentiation Source: UniProtKB
  4. positive regulation of catalytic activity Source: Ensembl
  5. positive regulation of DNA replication Source: Ensembl
  6. positive regulation of meiosis Source: UniProtKB
  7. protein homooligomerization Source: Ensembl
  8. regulation of exit from mitosis Source: UniProtKB
  9. single fertilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator, Developmental protein

Keywords - Biological processi

Fertilization

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleoplasmin-2
Gene namesi
Name:NPM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:7930. NPM2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasmic chromatin Source: UniProtKB
  2. nuclear chromatin Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31732.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 214214Nucleoplasmin-2PRO_0000219487Add
BLAST

Proteomic databases

MaxQBiQ86SE8.
PRIDEiQ86SE8.

PTM databases

PhosphoSiteiQ86SE8.

Expressioni

Gene expression databases

BgeeiQ86SE8.
CleanExiHS_NPM2.
ExpressionAtlasiQ86SE8. baseline.
GenevestigatoriQ86SE8.

Organism-specific databases

HPAiHPA041070.

Interactioni

Subunit structurei

Homopentamer, when bound to H2A-H2B dimers only. Homodecamer of two stacked pentamers, when bound to H2A-H2B dimers and H3-H4 tetramers simultaneously.1 Publication

Protein-protein interaction databases

BioGridi115641. 1 interaction.
IntActiQ86SE8. 1 interaction.
STRINGi9606.ENSP00000289820.

Structurei

Secondary structure

1
214
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 238Combined sources
Beta strandi29 – 324Combined sources
Beta strandi43 – 519Combined sources
Beta strandi60 – 656Combined sources
Beta strandi78 – 847Combined sources
Turni85 – 873Combined sources
Beta strandi90 – 989Combined sources
Beta strandi100 – 10910Combined sources
Beta strandi113 – 1208Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3T30X-ray1.90A/B/C/D/E/F/G/H/I/J14-122[»]
ProteinModelPortaliQ86SE8.
SMRiQ86SE8. Positions 15-121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 15224Acidic tract A2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi165 – 18016Bipartite nuclear localization signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi129 – 14416Poly-GluAdd
BLAST
Compositional biasi177 – 1804Poly-Lys
Compositional biasi182 – 1876Poly-Glu

Domaini

The acidic tract A2 mediates histone binding.1 Publication

Sequence similaritiesi

Belongs to the nucleoplasmin family.Curated

Phylogenomic databases

eggNOGiNOG78586.
GeneTreeiENSGT00440000034554.
HOGENOMiHOG000056457.
HOVERGENiHBG045601.
InParanoidiQ86SE8.
KOiK11277.
OMAiSTICLGE.
PhylomeDBiQ86SE8.
TreeFamiTF327704.

Family and domain databases

Gene3Di2.60.120.340. 1 hit.
InterProiIPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view]
PANTHERiPTHR22747. PTHR22747. 1 hit.
SUPFAMiSSF69203. SSF69203. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86SE8-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNLSSASSTE EKAVTTVLWG CELSQERRTW TFRPQLEGKQ SCRLLLHTIC
60 70 80 90 100
LGEKAKEEMH RVEILPPANQ EDKKMQPVTI ASLQASVLPM VSMVGVQLSP
110 120 130 140 150
PVTFQLRAGS GPVFLSGQER YEASDLTWEE EEEEEGEEEE EEEEDDEDED
160 170 180 190 200
ADISLEEQSP VKQVKRLVPQ KQASVAKKKK LEKEEEEIRA SVRDKSPVKK
210
AKATARAKKP GFKK
Length:214
Mass (Da):24,152
Last modified:June 1, 2003 - v1
Checksum:iEAE3BEF1DC8E1CC1
GO
Isoform 2 (identifier: Q86SE8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     123-214: ASDLTWEEEE...ARAKKPGFKK → KKAGKRRRGNKSQR

Note: No experimental confirmation available.

Show »
Length:136
Mass (Da):15,238
Checksum:iCEEABE3645C15B3B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei123 – 21492ASDLT…PGFKK → KKAGKRRRGNKSQR in isoform 2. 1 PublicationVSP_054261Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY262113 mRNA. Translation: AAP33134.1.
AY262114 mRNA. Translation: AAP33135.1.
AK094267 mRNA. Translation: BAG52852.1.
AC091171 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63731.1.
CH471080 Genomic DNA. Translation: EAW63732.1.
BC068078 mRNA. Translation: AAH68078.1.
CCDSiCCDS6018.1. [Q86SE8-1]
CCDS75703.1. [Q86SE8-2]
RefSeqiNP_001273609.1. NM_001286680.1. [Q86SE8-1]
NP_001273610.1. NM_001286681.1. [Q86SE8-2]
NP_877724.1. NM_182795.1. [Q86SE8-1]
UniGeneiHs.131055.

Genome annotation databases

EnsembliENST00000289820; ENSP00000289820; ENSG00000158806. [Q86SE8-1]
ENST00000381530; ENSP00000370941; ENSG00000158806. [Q86SE8-2]
ENST00000397940; ENSP00000381032; ENSG00000158806. [Q86SE8-1]
ENST00000518119; ENSP00000427741; ENSG00000158806. [Q86SE8-1]
ENST00000521157; ENSP00000429413; ENSG00000158806. [Q86SE8-1]
ENST00000615914; ENSP00000481018; ENSG00000158806. [Q86SE8-2]
ENST00000621538; ENSP00000481077; ENSG00000158806. [Q86SE8-1]
GeneIDi10361.
KEGGihsa:10361.
UCSCiuc003xac.3. human. [Q86SE8-1]
uc003xaf.3. human.

Polymorphism databases

DMDMi37537936.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY262113 mRNA. Translation: AAP33134.1 .
AY262114 mRNA. Translation: AAP33135.1 .
AK094267 mRNA. Translation: BAG52852.1 .
AC091171 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63731.1 .
CH471080 Genomic DNA. Translation: EAW63732.1 .
BC068078 mRNA. Translation: AAH68078.1 .
CCDSi CCDS6018.1. [Q86SE8-1 ]
CCDS75703.1. [Q86SE8-2 ]
RefSeqi NP_001273609.1. NM_001286680.1. [Q86SE8-1 ]
NP_001273610.1. NM_001286681.1. [Q86SE8-2 ]
NP_877724.1. NM_182795.1. [Q86SE8-1 ]
UniGenei Hs.131055.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3T30 X-ray 1.90 A/B/C/D/E/F/G/H/I/J 14-122 [» ]
ProteinModelPortali Q86SE8.
SMRi Q86SE8. Positions 15-121.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115641. 1 interaction.
IntActi Q86SE8. 1 interaction.
STRINGi 9606.ENSP00000289820.

PTM databases

PhosphoSitei Q86SE8.

Polymorphism databases

DMDMi 37537936.

Proteomic databases

MaxQBi Q86SE8.
PRIDEi Q86SE8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000289820 ; ENSP00000289820 ; ENSG00000158806 . [Q86SE8-1 ]
ENST00000381530 ; ENSP00000370941 ; ENSG00000158806 . [Q86SE8-2 ]
ENST00000397940 ; ENSP00000381032 ; ENSG00000158806 . [Q86SE8-1 ]
ENST00000518119 ; ENSP00000427741 ; ENSG00000158806 . [Q86SE8-1 ]
ENST00000521157 ; ENSP00000429413 ; ENSG00000158806 . [Q86SE8-1 ]
ENST00000615914 ; ENSP00000481018 ; ENSG00000158806 . [Q86SE8-2 ]
ENST00000621538 ; ENSP00000481077 ; ENSG00000158806 . [Q86SE8-1 ]
GeneIDi 10361.
KEGGi hsa:10361.
UCSCi uc003xac.3. human. [Q86SE8-1 ]
uc003xaf.3. human.

Organism-specific databases

CTDi 10361.
GeneCardsi GC08P021881.
HGNCi HGNC:7930. NPM2.
HPAi HPA041070.
MIMi 608073. gene.
neXtProti NX_Q86SE8.
PharmGKBi PA31732.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG78586.
GeneTreei ENSGT00440000034554.
HOGENOMi HOG000056457.
HOVERGENi HBG045601.
InParanoidi Q86SE8.
KOi K11277.
OMAi STICLGE.
PhylomeDBi Q86SE8.
TreeFami TF327704.

Miscellaneous databases

ChiTaRSi NPM2. human.
GenomeRNAii 10361.
NextBioi 39277.
PROi Q86SE8.
SOURCEi Search...

Gene expression databases

Bgeei Q86SE8.
CleanExi HS_NPM2.
ExpressionAtlasi Q86SE8. baseline.
Genevestigatori Q86SE8.

Family and domain databases

Gene3Di 2.60.120.340. 1 hit.
InterProi IPR004301. Nucleoplasmin.
IPR024057. Nucleoplasmin_core_dom.
[Graphical view ]
PANTHERi PTHR22747. PTHR22747. 1 hit.
SUPFAMi SSF69203. SSF69203. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Cerebellum.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Skin.
  6. "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.
  7. "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.

Entry informationi

Entry nameiNPM2_HUMAN
AccessioniPrimary (citable) accession number: Q86SE8
Secondary accession number(s): B3KSU0, D3DSQ8, Q6NVH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3