SFRS7

SRSF7
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2HVZ
Identifiers
Aliases	SRSF7, 9G8, AAG3, SFRS7, serine/arginine-rich splicing factor 7, serine and arginine rich splicing factor 7
External IDs	OMIM: 600572 MGI: 1926232 HomoloGene: 134446 GeneCards: SRSF7
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	38,751,494 bp[1]
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)[2]
End	80,207,307 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• zinc ion binding; • metal ion binding; • GO:0001948 protein binding; • nucleic acid binding; • RNA binding; • protein domain specific binding;
Cellular component	• cytoplasm; • nucleoplasm; • extracellular exosome; • cell nucleus; • nuclear speck;
Biological process	• mRNA splicing, via spliceosome; • termination of RNA polymerase II transcription; • mRNA transport; • mRNA processing; • mRNA export from nucleus; • negative regulation of mRNA splicing, via spliceosome; • mRNA 3'-end processing; • RNA export from nucleus; • RNA splicing; • cellular response to leukemia inhibitory factor; • transport; • regulation of alternative mRNA splicing, via spliceosome; • mRNA cis splicing, via spliceosome;
	Sources:Amigo / QuickGO
Orthologs
	6432
	225027
	ENSG00000115875
	ENSMUSG00000024097
	Q16629
	Q8BL97
	NM_001031684; NM_001195446; NM_006276; NM_001363802
	NM_001195485; NM_001195486; NM_001195487; NM_146083; NM_001360435
	NP_001026854; NP_001182375; NP_001350731
	NP_001182414; NP_001182415; NP_001182416; NP_666195; NP_001347364
	Wikidata
View/Edit Human	View/Edit Mouse

Serine/arginine-rich splicing factor 7 (SRSF7) also known as splicing factor, arginine/serine-rich 7 (SFRS7) or splicing factor 9G8 is a protein that in humans is encoded by the SRSF7 gene.[5]

Function

The protein encoded by this gene is a member of the serine/arginine (SR)-rich family of pre-mRNA splicing factors, which constitute part of the spliceosome. Each of these factors contains an RNA recognition motif (RRM) for binding RNA and an RS domain for binding other proteins. The RS domain is rich in serine and arginine residues and facilitates interaction between different SR splicing factors. In addition to being critical for mRNA splicing, the SR proteins have also been shown to be involved in mRNA export from the nucleus and in translation.[5]

Model organisms

Model organisms have been used in the study of SRSF7 function. A conditional knockout mouse line called Srsf7^{tm1a(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.[6] Male and female animals underwent a standardized phenotypic screen[7] to determine the effects of deletion.[8][9][10][11] Additional screens performed: - In-depth immunological phenotyping[12]

*Srsf7* knockout mouse phenotype
Characteristic	Phenotype
All data available at.[7][12]
Insulin	Normal
Homozygous viability at P14	Abnormal
Recessive lethal study	Abnormal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Salmonella infection	Normal
Epidermal Immune Composition	Normal

References

GRCh38: Ensembl release 89: ENSG00000115875 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000024097 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: SFRS7 splicing factor, arginine/serine-rich 7, 35kDa".
Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
"International Mouse Phenotyping Consortium".
Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.
White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
"Infection and Immunity Immunophenotyping (3i) Consortium".

Popielarz M, Cavaloc Y, Mattei MG, Gattoni R, Stévenin J (Jul 1995). "The gene encoding human splicing factor 9G8. Structure, chromosomal localization, and expression of alternatively processed transcripts". The Journal of Biological Chemistry. 270 (30): 17830–5. doi:10.1074/jbc.270.30.17830. PMID 7629084.
Cavaloc Y, Popielarz M, Fuchs JP, Gattoni R, Stévenin J (Jun 1994). "Characterization and cloning of the human splicing factor 9G8: a novel 35 kDa factor of the serine/arginine protein family". The EMBO Journal. 13 (11): 2639–49. doi:10.1002/j.1460-2075.1994.tb06554.x. PMC 395138. PMID 8013463.
Yuan Y, Li DM, Sun H (Aug 1998). "PIR1, a novel phosphatase that exhibits high affinity to RNA . ribonucleoprotein complexes". The Journal of Biological Chemistry. 273 (32): 20347–53. doi:10.1074/jbc.273.32.20347. PMID 9685386.
Lejeune F, Cavaloc Y, Stevenin J (Mar 2001). "Alternative splicing of intron 3 of the serine/arginine-rich protein 9G8 gene. Identification of flanking exonic splicing enhancers and involvement of 9G8 as a trans-acting factor". The Journal of Biological Chemistry. 276 (11): 7850–8. doi:10.1074/jbc.M009510200. PMID 11096110.
Nogues G, Kadener S, Cramer P, Bentley D, Kornblihtt AR (Nov 2002). "Transcriptional activators differ in their abilities to control alternative splicing". The Journal of Biological Chemistry. 277 (45): 43110–4. doi:10.1074/jbc.M208418200. PMID 12221105.
Hu D, Mayeda A, Trembley JH, Lahti JM, Kidd VJ (Mar 2003). "CDK11 complexes promote pre-mRNA splicing". The Journal of Biological Chemistry. 278 (10): 8623–9. doi:10.1074/jbc.M210057200. PMID 12501247.
Li J, Hawkins IC, Harvey CD, Jennings JL, Link AJ, Patton JG (Nov 2003). "Regulation of alternative splicing by SRrp86 and its interacting proteins". Molecular and Cellular Biology. 23 (21): 7437–47. doi:10.1128/MCB.23.21.7437-7447.2003. PMC 207616. PMID 14559993.
Yang L, Li N, Wang C, Yu Y, Yuan L, Zhang M, Cao X (Mar 2004). "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells". The Journal of Biological Chemistry. 279 (12): 11639–48. doi:10.1074/jbc.M312895200. PMID 14684736.
Ropers D, Ayadi L, Gattoni R, Jacquenet S, Damier L, Branlant C, Stévenin J (Jul 2004). "Differential effects of the SR proteins 9G8, SC35, ASF/SF2, and SRp40 on the utilization of the A1 to A5 splicing sites of HIV-1 RNA". The Journal of Biological Chemistry. 279 (29): 29963–73. doi:10.1074/jbc.M404452200. PMID 15123677.
Will CL, Schneider C, Hossbach M, Urlaub H, Rauhut R, Elbashir S, Tuschl T, Lührmann R (Jun 2004). "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome". RNA. 10 (6): 929–41. doi:10.1261/rna.7320604. PMC 1370585. PMID 15146077.
Dettwiler S, Aringhieri C, Cardinale S, Keller W, Barabino SM (Aug 2004). "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization" (PDF). The Journal of Biological Chemistry. 279 (34): 35788–97. doi:10.1074/jbc.M403927200. PMID 15169763. S2CID 39752996.
Lai MC, Tarn WY (Jul 2004). "Hypophosphorylated ASF/SF2 binds TAP and is present in messenger ribonucleoproteins". The Journal of Biological Chemistry. 279 (30): 31745–9. doi:10.1074/jbc.C400173200. PMID 15184380.
Huang Y, Yario TA, Steitz JA (Jun 2004). "A molecular link between SR protein dephosphorylation and mRNA export". Proceedings of the National Academy of Sciences of the United States of America. 101 (26): 9666–70. doi:10.1073/pnas.0403533101. PMC 470732. PMID 15210956.
Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Jacquenet S, Decimo D, Muriaux D, Darlix JL (2006). "Dual effect of the SR proteins ASF/SF2, SC35 and 9G8 on HIV-1 RNA splicing and virion production". Retrovirology. 2: 33. doi:10.1186/1742-4690-2-33. PMC 1180853. PMID 15907217.
van Abel D, Hölzel DR, Jain S, Lun FM, Zheng YW, Chen EZ, Sun H, Chiu RW, Lo YM, van Dijk M, Oudejans CB (2011). "SFRS7-mediated splicing of tau exon 10 is directly regulated by STOX1A in glial cells". PLOS ONE. 6 (7): e21994. doi:10.1371/journal.pone.0021994. PMC 3130792. PMID 21755018.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000115875 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000024097 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] "Entrez Gene: SFRS7 splicing factor, arginine/serine-rich 7, 35kDa".

[mgp_reference-6] Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.

[IMPCsearch_ref-7] "International Mouse Phenotyping Consortium".

[pmid21677750-8] Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.

[mouse_library-9] Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.

[mouse_for_all_reasons-10] Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. S2CID 18872015.

[pmid23870131-11] White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell. 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.

[iii_ref-12] "Infection and Immunity Immunophenotyping (3i) Consortium".

SFRS7

Function

Model organisms

References

Further reading