SRSF9_MOUSE
ID SRSF9_MOUSE Reviewed; 222 AA.
AC Q9D0B0; Q9CRN3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Serine/arginine-rich splicing factor 9;
DE AltName: Full=Splicing factor, arginine/serine-rich 9;
GN Name=Srsf9; Synonyms=Sfrs9;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP INTERACTION WITH KHDRBS3.
RX PubMed=11118435; DOI=10.1074/jbc.m006851200;
RA Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A.,
RA Stamm S.;
RT "The STAR/GSG family protein rSLM-2 regulates the selection of alternative
RT splice sites.";
RL J. Biol. Chem. 276:8665-8673(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [5]
RP STRUCTURE BY NMR OF 104-188.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in protein BAB31986.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Plays a role in constitutive splicing and can modulate the
CC selection of alternative splice sites. Represses the splicing of
CC MAPT/Tau exon 10 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KHDRBS3/SLM-2 (PubMed:11118435). Interacts with
CC HABP4. Interacts with NOL3/ARC/NOP30, NSEP1/YB-1/YB1, SAFB/SAFB1,
CC SRSF6/SFRS6, TRA2B/SFRS10 and C1QBP. May also interact with DUSP11/PIR1
CC (By similarity). {ECO:0000250|UniProtKB:Q13242,
CC ECO:0000269|PubMed:11118435}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; AK011621; BAB27740.1; -; mRNA.
DR EMBL; AK020084; BAB31986.1; -; mRNA.
DR EMBL; BC012217; AAH12217.1; -; mRNA.
DR CCDS; CCDS19587.1; -.
DR RefSeq; NP_079849.1; NM_025573.3.
DR PDB; 1WG4; NMR; -; A=104-188.
DR PDBsum; 1WG4; -.
DR AlphaFoldDB; Q9D0B0; -.
DR SMR; Q9D0B0; -.
DR BioGRID; 223767; 20.
DR IntAct; Q9D0B0; 2.
DR STRING; 10090.ENSMUSP00000031513; -.
DR iPTMnet; Q9D0B0; -.
DR PhosphoSitePlus; Q9D0B0; -.
DR EPD; Q9D0B0; -.
DR jPOST; Q9D0B0; -.
DR MaxQB; Q9D0B0; -.
DR PaxDb; Q9D0B0; -.
DR PeptideAtlas; Q9D0B0; -.
DR PRIDE; Q9D0B0; -.
DR ProteomicsDB; 258621; -.
DR Antibodypedia; 31480; 268 antibodies from 28 providers.
DR DNASU; 108014; -.
DR Ensembl; ENSMUST00000031513; ENSMUSP00000031513; ENSMUSG00000029538.
DR GeneID; 108014; -.
DR KEGG; mmu:108014; -.
DR UCSC; uc008zdq.1; mouse.
DR CTD; 8683; -.
DR MGI; MGI:104896; Srsf9.
DR VEuPathDB; HostDB:ENSMUSG00000029538; -.
DR eggNOG; KOG0105; Eukaryota.
DR GeneTree; ENSGT00940000156839; -.
DR HOGENOM; CLU_012062_34_0_1; -.
DR InParanoid; Q9D0B0; -.
DR OMA; SYIRVCP; -.
DR OrthoDB; 1315388at2759; -.
DR PhylomeDB; Q9D0B0; -.
DR TreeFam; TF106261; -.
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-72187; mRNA 3'-end processing.
DR Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR BioGRID-ORCS; 108014; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Srsf9; mouse.
DR EvolutionaryTrace; Q9D0B0; -.
DR PRO; PR:Q9D0B0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D0B0; protein.
DR Bgee; ENSMUSG00000029538; Expressed in renal corpuscle and 252 other tissues.
DR ExpressionAtlas; Q9D0B0; baseline and differential.
DR Genevisible; Q9D0B0; MM.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR CDD; cd12768; RRM2_SRSF9; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034995; SRSF9_RRM2.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..222
FT /note="Serine/arginine-rich splicing factor 9"
FT /id="PRO_0000081936"
FT DOMAIN 15..90
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 112..188
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 189..201
FT /note="Interaction with SAFB1"
FT /evidence="ECO:0000250"
FT REGION 190..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 215
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13242"
FT CONFLICT 209
FT /note="S -> N (in Ref. 1; BAB31986)"
FT /evidence="ECO:0000305"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1WG4"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:1WG4"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1WG4"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:1WG4"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:1WG4"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:1WG4"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:1WG4"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:1WG4"
SQ SEQUENCE 222 AA; 25661 MW; DF335337335AED19 CRC64;
MSSGWADERG GEGDGRIYVG NLPSDVREKD LEDLFYKYGR IREIELKNRH GLVPFAFVRF
EDPRDAEDAI YGRNGYDYGQ CRLRVEFPRT YGGRGGWPRG ARNGPPTRRS DFRVLVSGLP
PSGSWQDLKD HMREAGDVCY ADVQKDGMGM VEYLRKEDME YALRKLDDTK FRSHEGETSY
IRVYPERSTS YGYSRSRSGS RGRDSPYQSR GSPHYFSPFR PY
