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Advances in the Study of SR Protein Family
The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS d...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5172405/ https://www.ncbi.nlm.nih.gov/pubmed/15626328 http://dx.doi.org/10.1016/S1672-0229(03)01002-7 |
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author | Ma, Xiaoyun He, Fuchu |
author_facet | Ma, Xiaoyun He, Fuchu |
author_sort | Ma, Xiaoyun |
collection | PubMed |
description | The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS domain, and also possess special biochemical and immunological features. As to the functions of SR proteins, they facilitate the recruitment of the components of splicesome via protein-protein interaction to prompt the assembly of early splicesome; while in alternative splicing, tissue-specifically expressed SR protein along with the relative ratio of SR protein and heterogeneous nuclear ribonucleoprotein (hnRNP) is composed of two main regulative mechanisms for alternative splicing. Almost all of the biochemical functions are regulated by reversible phosphorylation. |
format | Online Article Text |
id | pubmed-5172405 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-51724052016-12-23 Advances in the Study of SR Protein Family Ma, Xiaoyun He, Fuchu Genomics Proteomics Bioinformatics Review The name of SR proteins is derived from their typical RS domain that is rich in serine (Ser, S) and arginine (Arg, R). They are conserved in evolution. Up to now, 10 members of the SR protein family have been identified in humans. SR proteins contain one or two RNA binding motifs aside from the RS domain, and also possess special biochemical and immunological features. As to the functions of SR proteins, they facilitate the recruitment of the components of splicesome via protein-protein interaction to prompt the assembly of early splicesome; while in alternative splicing, tissue-specifically expressed SR protein along with the relative ratio of SR protein and heterogeneous nuclear ribonucleoprotein (hnRNP) is composed of two main regulative mechanisms for alternative splicing. Almost all of the biochemical functions are regulated by reversible phosphorylation. Elsevier 2003-02 2016-11-28 /pmc/articles/PMC5172405/ /pubmed/15626328 http://dx.doi.org/10.1016/S1672-0229(03)01002-7 Text en . http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Review Ma, Xiaoyun He, Fuchu Advances in the Study of SR Protein Family |
title | Advances in the Study of SR Protein Family |
title_full | Advances in the Study of SR Protein Family |
title_fullStr | Advances in the Study of SR Protein Family |
title_full_unstemmed | Advances in the Study of SR Protein Family |
title_short | Advances in the Study of SR Protein Family |
title_sort | advances in the study of sr protein family |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5172405/ https://www.ncbi.nlm.nih.gov/pubmed/15626328 http://dx.doi.org/10.1016/S1672-0229(03)01002-7 |
work_keys_str_mv | AT maxiaoyun advancesinthestudyofsrproteinfamily AT hefuchu advancesinthestudyofsrproteinfamily |