SRSF2_MOUSE
ID SRSF2_MOUSE Reviewed; 221 AA.
AC Q62093; Q542L3; Q60701;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Serine/arginine-rich splicing factor 2;
DE AltName: Full=Protein PR264;
DE AltName: Full=Putative myelin regulatory factor 1;
DE Short=MRF-1;
DE AltName: Full=Splicing component, 35 kDa;
DE AltName: Full=Splicing factor SC35;
DE Short=SC-35;
DE AltName: Full=Splicing factor, arginine/serine-rich 2;
GN Name=Srsf2; Synonyms=Pr264, Sfrs10, Sfrs2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN MBP REGULATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7527040; DOI=10.1016/s0021-9258(18)47402-9;
RA Haque N.S., Buchberg A.M., Khalili K.;
RT "Isolation and characterization of MRF-1, a brain-derived DNA-binding
RT protein with a capacity to regulate expression of myelin basic protein
RT gene.";
RL J. Biol. Chem. 269:31149-31156(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9774382; DOI=10.1074/jbc.273.43.27761;
RA Yang L., Embree L.J., Tsai S., Hickstein D.D.;
RT "Oncoprotein TLS interacts with serine-arginine proteins involved in RNA
RT splicing.";
RL J. Biol. Chem. 273:27761-27764(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Bone marrow, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RC STRAIN=129/Sv; TISSUE=Liver;
RA Gaillard C., Perbal B.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-206; SER-208 AND
RP SER-212, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH BRDT.
RX PubMed=22570411; DOI=10.1093/nar/gks342;
RA Berkovits B.D., Wang L., Guarnieri P., Wolgemuth D.J.;
RT "The testis-specific double bromodomain-containing protein BRDT forms a
RT complex with multiple spliceosome components and is required for mRNA
RT splicing and 3'-UTR truncation in round spermatids.";
RL Nucleic Acids Res. 40:7162-7175(2012).
CC -!- FUNCTION: Necessary for the splicing of pre-mRNA. It is required for
CC formation of the earliest ATP-dependent splicing complex and interacts
CC with spliceosomal components bound to both the 5'- and 3'-splice sites
CC during spliceosome assembly. It also is required for ATP-dependent
CC interactions of both U1 and U2 snRNPs with pre-mRNA (By similarity).
CC Can bind to the myelin basic protein (MBP) gene MB3 regulatory region
CC and increase transcription of the mbp promoter in cells derived from
CC the CNS. The phosphorylated form (by SRPK2) is required for cellular
CC apoptosis in response to cisplatin treatment (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:7527040}.
CC -!- SUBUNIT: Interacts with CCNL1 and CCNL2. Interacts with SCAF11.
CC Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus)
CC (By similarity). In vitro, self-associates and binds SRSF1/SFRS1
CC (ASF/SF2), SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12.
CC Interacts with BRDT. {ECO:0000250, ECO:0000269|PubMed:22570411}.
CC -!- INTERACTION:
CC Q62093; Q99J95: Cdk9; NbExp=3; IntAct=EBI-2550402, EBI-2654963;
CC Q62093; Q8R409: Hexim1; NbExp=4; IntAct=EBI-2550402, EBI-6261031;
CC Q62093; P08775: Polr2a; NbExp=3; IntAct=EBI-2550402, EBI-2549849;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleoplasm
CC {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Phosphorylation by
CC SRPK2 provokes its redistribution from the nuclear speckle to
CC nucleoplasm. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all the tissues examined; liver,
CC kidney, spleen, heart, lung and brain. {ECO:0000269|PubMed:7527040}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC Phosphorylated by SRPK2 and this causes its redistribution from the
CC nuclear speckle to nucleoplasm and controls cell fate decision in
CC response to cisplatin treatment. KAT5/TIP60 inhibits its
CC phosphorylation by preventing SRPK2 nuclear translocation (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylation on Lys-52 by KAT5/TIP60 promotes its proteasomal
CC degradation. This effect is counterbalanced by HDAC6, which positively
CC controls SRSF2 protein level by deacetylating it and preventing its
CC proteasomal degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA64595.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U14648; AAA64595.1; ALT_FRAME; mRNA.
DR EMBL; AF077858; AAC71000.1; -; mRNA.
DR EMBL; AK086103; BAC39610.1; -; mRNA.
DR EMBL; AK088042; BAC40111.1; -; mRNA.
DR EMBL; AK165670; BAE38330.1; -; mRNA.
DR EMBL; BC005493; AAH05493.1; -; mRNA.
DR EMBL; X98511; CAA67134.1; -; Genomic_DNA.
DR CCDS; CCDS25680.1; -.
DR PIR; A55335; A55335.
DR RefSeq; NP_035488.1; NM_011358.2.
DR RefSeq; XP_011247137.1; XM_011248835.2.
DR AlphaFoldDB; Q62093; -.
DR SMR; Q62093; -.
DR BioGRID; 203188; 35.
DR DIP; DIP-44831N; -.
DR IntAct; Q62093; 10.
DR MINT; Q62093; -.
DR STRING; 10090.ENSMUSP00000090059; -.
DR iPTMnet; Q62093; -.
DR PhosphoSitePlus; Q62093; -.
DR SwissPalm; Q62093; -.
DR EPD; Q62093; -.
DR jPOST; Q62093; -.
DR MaxQB; Q62093; -.
DR PaxDb; Q62093; -.
DR PeptideAtlas; Q62093; -.
DR PRIDE; Q62093; -.
DR ProteomicsDB; 257413; -.
DR DNASU; 20382; -.
DR Ensembl; ENSMUST00000092404; ENSMUSP00000090059; ENSMUSG00000034120.
DR Ensembl; ENSMUST00000136914; ENSMUSP00000120086; ENSMUSG00000034120.
DR Ensembl; ENSMUST00000190993; ENSMUSP00000140016; ENSMUSG00000034120.
DR GeneID; 20382; -.
DR KEGG; mmu:20382; -.
DR UCSC; uc007mmn.2; mouse.
DR CTD; 6427; -.
DR MGI; MGI:98284; Srsf2.
DR VEuPathDB; HostDB:ENSMUSG00000034120; -.
DR eggNOG; KOG4207; Eukaryota.
DR GeneTree; ENSGT00940000154883; -.
DR HOGENOM; CLU_012062_10_3_1; -.
DR InParanoid; Q62093; -.
DR OMA; PLIRCDV; -.
DR OrthoDB; 1524134at2759; -.
DR PhylomeDB; Q62093; -.
DR TreeFam; TF106262; -.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 20382; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Srsf2; mouse.
DR PRO; PR:Q62093; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q62093; protein.
DR Bgee; ENSMUSG00000034120; Expressed in dorsal pancreas and 256 other tissues.
DR ExpressionAtlas; Q62093; baseline and differential.
DR Genevisible; Q62093; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035061; C:interchromatin granule; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005726; C:perichromatin fibrils; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:MGI.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0033197; P:response to vitamin E; IEA:Ensembl.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR034893; SRSF2-like.
DR PANTHER; PTHR23147:SF119; PTHR23147:SF119; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT CHAIN 2..221
FT /note="Serine/arginine-rich splicing factor 2"
FT /id="PRO_0000081919"
FT DOMAIN 14..92
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 92..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..187
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 22
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT CONFLICT 66..67
FT /note="RD -> PH (in Ref. 1; AAA64595)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="M -> L (in Ref. 1; AAA64595)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="A -> E (in Ref. 1; AAA64595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 221 AA; 25476 MW; 68121AC4D35714FA CRC64;
MSYGRPPPDV EGMTSLKVDN LTYRTSPDTL RRVFEKYGRV GDVYIPRDRY TKESRGFAFV
RFHDKRDAED AMDAMDGAVL DGRELRVQMA RYGRPPDSHH SRRGPPPRRY GGGGYGRRSR
SPRRRRRSRS RSRSRSRSRS RSRYSRSKSR SRTRSRSRST SKSRSARRSK SKSSSVSRSR
SRSRSRSRSR SPPPVSKRES KSRSRSKSPP KSPEEEGAVS S
