SRSF2_RAT
ID SRSF2_RAT Reviewed; 221 AA.
AC Q6PDU1;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Serine/arginine-rich splicing factor 2;
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=Sfrs2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 [2]
RP INTERACTION WITH CCNL1.
RX PubMed=11683997; DOI=10.1016/s0896-6273(01)00465-2;
RA Berke J.D., Sgambato V., Zhu P.-P., Lavoie B., Vincent M., Krause M.,
RA Hyman S.E.;
RT "Dopamine and glutamate induce distinct striatal splice forms of Ania-6, an
RT RNA polymerase II-associated cyclin.";
RL Neuron 32:277-287(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-26; SER-189; SER-191;
RP SER-206; SER-208 AND SER-212, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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. The phosphorylated
CC form (by SRPK2) is required for cellular apoptosis in response to
CC cisplatin treatment (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: In vitro, self-associates and binds SRSF1/SFRS1 (ASF/SF2),
CC SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with
CC CCNL2. Interacts with SCAF11. Interacts with ZRSR2/U2AF1-RS2. Interacts
CC with CCDC55 (via C-terminus). Interacts with BRDT (By similarity).
CC Interacts with CCNL1. {ECO:0000250, ECO:0000269|PubMed:11683997}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC Phosphorylated by SRPK2 and this controls cell fate decision in
CC response to cisplatin treatment. SRSF2 and SRPK2 cooperate to induce
CC apoptosis through regulation of the splicing switch of caspase-8 pre-
CC mRNA and in the absence of SRPK2, cisplatin-treated cells accumulate in
CC G2/M phase. KAT5/TIP60 inhibits its phosphorylation by preventing SRPK2
CC nuclear translocation (By 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}.
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DR EMBL; BC058508; AAH58508.1; -; mRNA.
DR RefSeq; NP_001009720.1; NM_001009720.2.
DR RefSeq; XP_006247875.1; XM_006247813.3.
DR RefSeq; XP_008766604.1; XM_008768382.1.
DR AlphaFoldDB; Q6PDU1; -.
DR SMR; Q6PDU1; -.
DR BioGRID; 268944; 2.
DR IntAct; Q6PDU1; 4.
DR MINT; Q6PDU1; -.
DR STRING; 10116.ENSRNOP00000059012; -.
DR iPTMnet; Q6PDU1; -.
DR PhosphoSitePlus; Q6PDU1; -.
DR jPOST; Q6PDU1; -.
DR PaxDb; Q6PDU1; -.
DR PRIDE; Q6PDU1; -.
DR Ensembl; ENSRNOT00000067739; ENSRNOP00000059012; ENSRNOG00000000248.
DR GeneID; 494445; -.
DR KEGG; rno:494445; -.
DR CTD; 6427; -.
DR RGD; 1359422; Srsf2.
DR eggNOG; KOG4207; Eukaryota.
DR GeneTree; ENSGT00940000154883; -.
DR HOGENOM; CLU_012062_10_3_1; -.
DR InParanoid; Q6PDU1; -.
DR OMA; PLIRCDV; -.
DR OrthoDB; 1524134at2759; -.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-RNO-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q6PDU1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000000248; Expressed in thymus and 20 other tissues.
DR Genevisible; Q6PDU1; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0035061; C:interchromatin granule; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005726; C:perichromatin fibrils; IDA:RGD.
DR GO; GO:0005681; C:spliceosomal complex; ISO:RGD.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:RGD.
DR GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000278; P:mitotic cell cycle; IEP:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
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_0000081921"
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:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01130"
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
