ID   SPF45_HUMAN             Reviewed;         401 AA.
AC   Q96I25; Q96GY6;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-JAN-2012, entry version 93.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, Testis, and Uterus;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH THE SPLICEOSOME.
RX   MEDLINE=98400255; 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
RT   of the multi-protein spliceosome complex.";
RL   Nat. Genet. 20:46-50(1998).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=22011779; PubMed=12015979; DOI=10.1016/S0092-8674(02)00730-4;
RA   Lallena M.J., Chalmers K.J., Llamazares S., Lamond A.I., Valcarcel J.;
RT   "Splicing regulation at the second catalytic step by Sex-lethal
RT   involves 3' splice site recognition by SPF45.";
RL   Cell 109:285-296(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-71 AND SER-155, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-204, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17287340; DOI=10.1073/pnas.0611217104;
RA   Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
RT   "Global proteomic profiling of phosphopeptides using electron transfer
RT   dissociation tandem mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=T-cell;
RX   PubMed=19367720; DOI=10.1021/pr800500r;
RA   Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT   "Phosphorylation analysis of primary human T lymphocytes using
RT   sequential IMAC and titanium oxide enrichment.";
RL   J. Proteome Res. 7:5167-5176(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18318008; DOI=10.1002/pmic.200700884;
RA   Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA   Zou H., Gu J.;
RT   "Large-scale phosphoproteome analysis of human liver tissue by
RT   enrichment and fractionation of phosphopeptides with strong anion
RT   exchange chromatography.";
RL   Proteomics 8:1346-1361(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-169, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-169, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Splice factor that binds to the single stranded 3'AG at
CC       the exon/intron border and promotes its utilization in the second
CC       catalytic step. Involved in the regulation of alternative splicing
CC       and the utilization of cryptic splice sites. Promotes the
CC       utilization of a cryptic splice site created by the beta-110
CC       mutation in the HBB gene. The resulting frameshift leads to sickle
CC       cell anemia.
CC   -!- SUBUNIT: Binds SXL. Associates with the spliceosome.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; BC007871; AAH07871.1; -; mRNA.
DR   EMBL; BC009064; AAH09064.1; -; mRNA.
DR   EMBL; BC039322; AAH39322.1; -; mRNA.
DR   IPI; IPI00176706; -.
DR   RefSeq; NP_001139019.1; NM_001145547.1.
DR   RefSeq; NP_116294.1; NM_032905.4.
DR   UniGene; Hs.498548; -.
DR   PDB; 2PE8; X-ray; 2.00 A; A=301-401.
DR   PDB; 2PEH; X-ray; 2.11 A; A/B=301-401.
DR   PDBsum; 2PE8; -.
DR   PDBsum; 2PEH; -.
DR   ProteinModelPortal; Q96I25; -.
DR   SMR; Q96I25; 301-401.
DR   DIP; DIP-29409N; -.
DR   IntAct; Q96I25; 6.
DR   MINT; MINT-3053773; -.
DR   STRING; Q96I25; -.
DR   PhosphoSite; Q96I25; -.
DR   DMDM; 34925383; -.
DR   PeptideAtlas; Q96I25; -.
DR   PRIDE; Q96I25; -.
DR   Ensembl; ENST00000379888; ENSP00000369218; ENSG00000134453.
DR   Ensembl; ENST00000446108; ENSP00000388638; ENSG00000134453.
DR   GeneID; 84991; -.
DR   KEGG; hsa:84991; -.
DR   UCSC; uc001ijb.1; human.
DR   CTD; 84991; -.
DR   GeneCards; GC10P006130; -.
DR   H-InvDB; HIX0008618; -.
DR   HGNC; HGNC:16944; RBM17.
DR   HPA; HPA037477; -.
DR   MIM; 606935; gene.
DR   neXtProt; NX_Q96I25; -.
DR   GeneTree; ENSGT00390000008837; -.
DR   HOGENOM; HBG608718; -.
DR   HOVERGEN; HBG059363; -.
DR   InParanoid; Q96I25; -.
DR   OMA; SDERQIV; -.
DR   OrthoDB; EOG48SGTF; -.
DR   PhylomeDB; Q96I25; -.
DR   NextBio; 75577; -.
DR   ArrayExpress; Q96I25; -.
DR   Bgee; Q96I25; -.
DR   CleanEx; HS_RBM17; -.
DR   Genevestigator; Q96I25; -.
DR   GermOnline; ENSG00000134453; Homo sapiens.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR003954; RRM_dom_euk.
DR   InterPro; IPR016967; Splicing_factor_SPF45.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   KO; K12840; -.
DR   Pfam; PF01585; G-patch; 1.
DR   PIRSF; PIRSF031066; Splicing_factor_SPF45; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00361; RRM_1; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50102; RRM; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome;
KW   Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; RNA-binding; Spliceosome.
FT   CHAIN         1    401       Splicing factor 45.
FT                                /FTId=PRO_0000081903.
FT   DOMAIN      235    283       G-patch.
FT   DOMAIN      306    385       RRM.
FT   MOD_RES      21     21       N6-acetyllysine.
FT   MOD_RES      71     71       Phosphothreonine.
FT   MOD_RES     155    155       Phosphoserine.
FT   MOD_RES     169    169       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine.
FT   CONFLICT    214    214       Y -> H (in Ref. 1; AAH09064).
FT   STRAND      305    313
FT   HELIX       323    329
FT   HELIX       330    333
FT   STRAND      336    343
FT   TURN        349    351
FT   STRAND      352    361
FT   HELIX       362    372
FT   STRAND      383    386
FT   HELIX       389    393
SQ   SEQUENCE   401 AA;  44962 MW;  99FA8C5E5E998554 CRC64;
     MSLYDDLGVE TSDSKTEGWS KNFKLLQSQL QVKKAALTQA KSQRTKQSTV LAPVIDLKRG
     GSSDDRQIVD TPPHVAAGLK DPVPSGFSAG EVLIPLADEY DPMFPNDYEK VVKRQREERQ
     RQRELERQKE IEEREKRRKD RHEASGFARR PDPDSDEDED YERERRKRSM GGAAIAPPTS
     LVEKDKELPR DFPYEEDSRP RSQSSKAAIP PPVYEEQDRP RSPTGPSNSF LANMGGTVAH
     KIMQKYGFRE GQGLGKHEQG LSTALSVEKT SKRGGKIIVG DATEKDASKK SDSNPLTEIL
     KCPTKVVLLR NMVGAGEVDE DLEVETKEEC EKYGKVGKCV IFEIPGAPDD EAVRIFLEFE
     RVESAIKAVV DLNGRYFGGR VVKACFYNLD KFRVLDLAEQ V
//