Search by BoMiProt ID - Bomi9038

Primary Information

BoMiProt ID Bomi9038
Protein Name Serine/arginine-rich splicing factor 3/Splicing factor, arginine/serine-rich 3
Organism Bos taurus
Uniprot IDQ3SZR8
Milk FractionWhey
Ref Sequence ID NP_001029872.1
Aminoacid Length 164
Molecular Weight 19330
FASTA Sequence Download
Gene Name SRSF3
Gene ID 540276
Protein Existence Status Reviewed

Secondary Information

Presence in other biological fluids/tissue/cells abdominal lymph node
Protein Function Serine/arginine-rich splicing factor 3 (SRSF3), previously named as SRp20 and SFRS3, is the smallest member of serine/arginine-rich (SR) protein family, well known for its regulatory roles in RNA metabolism and functions, such as pre-mRNA splicing, mRNA 3′ end processing, mRNA export from nucleus and cap-independent translation. SRSF3 was also implicated in the regulation of chromatin structure and function because of its association with interphase chromatin but not with hyperphosphorylated mitotic chromosomes.
PTMs N-acetylation at Methionine,Phosphorylation at Serine by CLK1, CLK2, CLK3 and CLK4
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions 78-164
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments Serine/arginine-rich splicing factor 3 (SRSF3) is overexpressed in human ovarian cancer and the overexpression of SRSF3 was required for ovarian cancer cell growth and survival.
Bibliography 1.He X, Zhang P. Serine/arginine-rich splicing factor 3 (SRSF3) regulates homologous recombination-mediated DNA repair. Mol Cancer. 2015 Aug 19;14:158. doi: 10.1186/s12943-015-0422-1. PMID: 26282282; PMCID: PMC4539922. 2.Sen S, Talukdar I, Webster NJ. SRp20 and CUG-BP1 modulate insulin receptor exon 11 alternative splicing. Mol Cell Biol. 2009;29(3):871–80. doi: 10.1128/MCB.01709-08. 3. Galiana-Arnoux D, Lejeune F, Gesnel MC, Stevenin J, Breathnach R, Del Gatto-Konczak F. The CD44 alternative v9 exon contains a splicing enhancer responsive to the SR proteins 9G8, ASF/SF2, and SRp20. J Biol Chem. 2003;278(35):32943–53. doi: 10.1074/jbc.M301090200. 4.Jumaa H, Nielsen PJ. Regulation of SRp20 exon 4 splicing. Biochim Biophys Acta. 2000;1494(1–2):137–43. doi: 10.1016/S0167-4781(00)00233-5. 5.Kuo BA, Uporova TM, Liang H, Bennett VD, Tuan RS, Norton PA. Alternative splicing during chondrogenesis: modulation of fibronectin exon EIIIA splicing by SR proteins. J Cell Biochem. 2002;86(1):45–55. doi: 10.1002/jcb.10188. 6.Cui M, Allen MA, Larsen A, Macmorris M, Han M, Blumenthal T. Genes involved in pre-mRNA 3′-end formation and transcription termination revealed by a lin-15 operon Muv suppressor screen. Proc Natl Acad Sci U S A. 2008;105(43):16665–70. doi: 10.1073/pnas.0807104105. 7.Lou H, Neugebauer KM, Gagel RF, Berget SM. Regulation of alternative polyadenylation by U1 snRNPs and SRp20. Mol Cell Biol. 1998;18(9):4977–85. 8.Escudero-Paunetto L, Li L, Hernandez FP, Sandri-Goldin RM. SR proteins SRp20 and 9G8 contribute to efficient export of herpes simplex virus 1 mRNAs. Virology. 2010;401(2):155–64. doi: 10.1016/j.virol.2010.02.023. 9. Hautbergue GM, Hung ML, Golovanov AP, Lian LY, Wilson SA. Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP. Proc Natl Acad Sci U S A. 2008;105(13):5154–9. doi: 10.1073/pnas.0709167105. 10.Huang Y, Steitz JA. Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol Cell. 2001;7(4):899–905. doi: 10.1016/S1097-2765(01)00233-7. 11. Kim J, Park RY, Chen JK, Kim J, Jeong S, Ohn T. Splicing factor SRSF3 represses the translation of programmed cell death 4 mRNA by associating with the 5′-UTR region. Cell Death Differ. 2014;21(3):481–90. doi: 10.1038/cdd.2013.171. 12.Bedard KM, Daijogo S, Semler BL. A nucleo-cytoplasmic SR protein functions in viral IRES-mediated translation initiation. EMBO J. 2007;26(2):459–67. doi: 10.1038/sj.emboj.7601494. 13.Loomis RJ, Naoe Y, Parker JB, Savic V, Bozovsky MR, Macfarlan T, et al. Chromatin binding of SRp20 and ASF/SF2 and dissociation from mitotic chromosomes is modulated by histone H3 serine 10 phosphorylation. Mol Cell. 2009;33(4):450–61. doi: 10.1016/j.molcel.2009.02.003.