SPF45_MOUSE
ID SPF45_MOUSE Reviewed; 405 AA.
AC Q8JZX4; A2AP41; O75939;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Splicing factor 45;
DE AltName: Full=45 kDa-splicing factor;
DE AltName: Full=RNA-binding motif protein 17;
GN Name=Rbm17; Synonyms=Spf45;
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].
RX PubMed=9731529; DOI=10.1038/1700;
RA Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P.,
RA Sleeman J., Lamond A.I., Mann M.;
RT "Mass spectrometry and EST-database searching allows characterization of
RT the multi-protein spliceosome complex.";
RL Nat. Genet. 20:46-50(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Splice factor that binds to the single-stranded 3'AG at the
CC exon/intron border and promotes its utilization in the second catalytic
CC step. Involved in the regulation of alternative splicing and the
CC utilization of cryptic splice sites (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds SXL. Associates with the spliceosome. Interacts with
CC SF3B1, SF1 and U2AF2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AF083384; AAC64085.1; -; mRNA.
DR EMBL; AL831794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034896; AAH34896.1; -; mRNA.
DR CCDS; CCDS15684.1; -.
DR RefSeq; NP_690037.1; NM_152824.1.
DR AlphaFoldDB; Q8JZX4; -.
DR BMRB; Q8JZX4; -.
DR SMR; Q8JZX4; -.
DR BioGRID; 218413; 2.
DR DIP; DIP-60651N; -.
DR IntAct; Q8JZX4; 2.
DR STRING; 10090.ENSMUSP00000041831; -.
DR iPTMnet; Q8JZX4; -.
DR PhosphoSitePlus; Q8JZX4; -.
DR EPD; Q8JZX4; -.
DR jPOST; Q8JZX4; -.
DR MaxQB; Q8JZX4; -.
DR PaxDb; Q8JZX4; -.
DR PeptideAtlas; Q8JZX4; -.
DR PRIDE; Q8JZX4; -.
DR ProteomicsDB; 261133; -.
DR ABCD; Q8JZX4; 1 sequenced antibody.
DR Antibodypedia; 43907; 130 antibodies from 25 providers.
DR DNASU; 76938; -.
DR Ensembl; ENSMUST00000040314; ENSMUSP00000041831; ENSMUSG00000037197.
DR GeneID; 76938; -.
DR KEGG; mmu:76938; -.
DR UCSC; uc008iio.1; mouse.
DR CTD; 84991; -.
DR MGI; MGI:1924188; Rbm17.
DR VEuPathDB; HostDB:ENSMUSG00000037197; -.
DR eggNOG; KOG1996; Eukaryota.
DR GeneTree; ENSGT00790000123099; -.
DR HOGENOM; CLU_044888_0_0_1; -.
DR InParanoid; Q8JZX4; -.
DR OMA; EERFGNN; -.
DR OrthoDB; 1101846at2759; -.
DR PhylomeDB; Q8JZX4; -.
DR TreeFam; TF313987; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 76938; 23 hits in 110 CRISPR screens.
DR ChiTaRS; Rbm17; mouse.
DR PRO; PR:Q8JZX4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8JZX4; protein.
DR Bgee; ENSMUSG00000037197; Expressed in embryonic post-anal tail and 262 other tissues.
DR ExpressionAtlas; Q8JZX4; baseline and differential.
DR Genevisible; Q8JZX4; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR CDD; cd12647; RRM_UHM_SPF45; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR040052; RBM17.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR034653; SPF45_RRM.
DR PANTHER; PTHR13288; PTHR13288; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF031066; Splicing_factor_SPF45; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Spliceosome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CHAIN 2..405
FT /note="Splicing factor 45"
FT /id="PRO_0000081904"
FT DOMAIN 235..283
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 310..389
FT /note="RRM"
FT REGION 57..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
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:Q96I25"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 41
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96I25"
SQ SEQUENCE 405 AA; 45304 MW; 2BCAE02BFA7AB8CA CRC64;
MSLYDDLGVE TSDSKTEGWS KNFKLLQSQL QVKKAALTQA KSQRTKQSTV LAPVIDLKRG
GSSDDRQIAD TPPHVAAGLK DPVPSGFSAG EVLIPLADEY DPMFPNDYEK VVKRQREERQ
RQRELERQKE IEEREKRRKD RHEASGFSRR PDPDSDEDED YERERRKRSM GGAAIAPPTS
LVEKDKELPR DFPYEEDSRP RSQSSKAAIP PPVYEEPDRP RSPTGPSNSF LANMGGTVAH
KIMQKYGFRE GQGLGKHEQG LSTALSVEKT SKRGGKIIVG DATEKGEAQD ASKKSDSNPL
TEILKCPTKV VLLRNMVGAG EVDEDLEVET KEECEKYGKV GKCVIFEIPG APDDEAVRIF
LEFERVESAI KAVVDLNGRY FGGRVVKACF YNLDKFRVLD LAEQV
