Thr199 phosphorylation targets nucleophosmin to nuclear speckles and represses pre-mRNA processing (Q28590167)

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14 January 2020

title

Thr199 phosphorylation targets nucleophosmin to nuclear speckles and represses pre-mRNA processing (English)

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14 January 2020

0 references

1 reference

GOA release 2020-03-11

Serine and arginine-rich splicing factor 2

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GOA release 2020-03-11

author

Pheruza Tarapore

1

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14 January 2020

Kazuya Shinmura

2

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author name string

Hitoshi Suzuki

3

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14 January 2020

Yukari Tokuyama

4

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14 January 2020

Song-Hee Kim

5

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Akila Mayeda

6

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14 January 2020

Kenji Fukasawa

7

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language of work or name

English

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publication date

19 December 2005

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volume

580

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issue

2

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page(s)

399-409

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Silver staining, immunofluorescence, and immunoelectron microscopic localization of nucleolar phosphoproteins B23 and C23

14 January 2020

cites work

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Nucleolar protein B23.1 binds to retinoblastoma protein and synergistically stimulates DNA polymerase alpha activity

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Major nucleolar proteins shuttle between nucleus and cytoplasm

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Specific phosphorylation of nucleophosmin on Thr(199) by cyclin-dependent kinase 2-cyclin E and its role in centrosome duplication.

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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

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B23/nucleophosmin serine 4 phosphorylation mediates mitotic functions of polo-like kinase 1.

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Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo

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Activation of pre-mRNA splicing by human RNPS1 is regulated by CK2 phosphorylation.

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The 35-kDa mammalian splicing factor SC35 mediates specific interactions between U1 and U2 small nuclear ribonucleoprotein particles at the 3' splice site

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Intron-dependent recruitment of pre-mRNA splicing factors to sites of transcription

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21 January 2018

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21 January 2018

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Identifiers

DOI

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14 January 2020

2 references

31 January 2017