SPF45_HUMAN
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 03-AUG-2022, entry version 180.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PARTIAL PROTEIN SEQUENCE, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH THE SPLICEOSOME.
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 [3]
RP FUNCTION.
RX 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 involves 3'
RT 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
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-169, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; SER-169 AND SER-222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-71; SER-155; SER-169;
RP THR-237; SER-266; SER-291 AND SER-293, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-222, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-24; LYS-33; LYS-41;
RP LYS-58; LYS-256 AND LYS-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 301-401 IN COMPLEX WITH SF3B1,
RP FUNCTION, INTERACTION WITH SF3B1; SF1 AND U2AF2, AND MUTAGENESIS OF
RP ASP-319; ARG-375; TYR-376 AND PHE-377.
RX PubMed=17589525; DOI=10.1038/nsmb1260;
RA Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J.,
RA Sattler M.;
RT "U2AF-homology motif interactions are required for alternative splicing
RT regulation by SPF45.";
RL Nat. Struct. Mol. Biol. 14:620-629(2007).
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. Promotes the utilization of a
CC cryptic splice site created by the beta-110 mutation in the HBB gene.
CC The resulting frameshift leads to sickle cell anemia.
CC {ECO:0000269|PubMed:12015979, ECO:0000269|PubMed:17589525}.
CC -!- SUBUNIT: Binds SXL. Associates with the spliceosome. Interacts with
CC SF3B1, SF1 and U2AF2. {ECO:0000269|PubMed:17589525,
CC ECO:0000269|PubMed:9731529}.
CC -!- INTERACTION:
CC Q96I25; P54253: ATXN1; NbExp=5; IntAct=EBI-740272, EBI-930964;
CC Q96I25; P27797: CALR; NbExp=3; IntAct=EBI-740272, EBI-1049597;
CC Q96I25; Q8IYT3: CCDC170; NbExp=3; IntAct=EBI-740272, EBI-2808089;
CC Q96I25; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-740272, EBI-10175300;
CC Q96I25; Q53EZ4: CEP55; NbExp=8; IntAct=EBI-740272, EBI-747776;
CC Q96I25; O43143: DHX15; NbExp=11; IntAct=EBI-740272, EBI-1237044;
CC Q96I25; P36957: DLST; NbExp=3; IntAct=EBI-740272, EBI-351007;
CC Q96I25; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-740272, EBI-10175124;
CC Q96I25; Q08379: GOLGA2; NbExp=8; IntAct=EBI-740272, EBI-618309;
CC Q96I25; O75031: HSF2BP; NbExp=3; IntAct=EBI-740272, EBI-7116203;
CC Q96I25; Q9H0B3: IQCN; NbExp=3; IntAct=EBI-740272, EBI-745878;
CC Q96I25; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-740272, EBI-1055945;
CC Q96I25; P16284: PECAM1; NbExp=3; IntAct=EBI-740272, EBI-716404;
CC Q96I25; Q9BZL4: PPP1R12C; NbExp=3; IntAct=EBI-740272, EBI-721802;
CC Q96I25; Q9BZL4-5: PPP1R12C; NbExp=3; IntAct=EBI-740272, EBI-10289057;
CC Q96I25; Q2TAL8: QRICH1; NbExp=4; IntAct=EBI-740272, EBI-2798044;
CC Q96I25; P21673: SAT1; NbExp=13; IntAct=EBI-740272, EBI-711613;
CC Q96I25; Q15637: SF1; NbExp=8; IntAct=EBI-740272, EBI-744603;
CC Q96I25; Q15637-4: SF1; NbExp=3; IntAct=EBI-740272, EBI-12223157;
CC Q96I25; Q15428: SF3A2; NbExp=2; IntAct=EBI-740272, EBI-2462271;
CC Q96I25; O75533: SF3B1; NbExp=3; IntAct=EBI-740272, EBI-876542;
CC Q96I25; O75533-1: SF3B1; NbExp=3; IntAct=EBI-740272, EBI-15565798;
CC Q96I25; Q8IWZ8: SUGP1; NbExp=2; IntAct=EBI-740272, EBI-2691671;
CC Q96I25; P26368: U2AF2; NbExp=2; IntAct=EBI-740272, EBI-742339;
CC Q96I25; O76024: WFS1; NbExp=3; IntAct=EBI-740272, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9731529}.
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DR EMBL; BC007871; AAH07871.1; -; mRNA.
DR EMBL; BC009064; AAH09064.1; -; mRNA.
DR EMBL; BC039322; AAH39322.1; -; mRNA.
DR CCDS; CCDS7077.1; -.
DR RefSeq; NP_001139019.1; NM_001145547.1.
DR RefSeq; NP_116294.1; NM_032905.4.
DR PDB; 2PE8; X-ray; 2.00 A; A=301-401.
DR PDB; 2PEH; X-ray; 2.11 A; A/B=301-401.
DR PDB; 5LSO; X-ray; 2.22 A; A/B=301-400.
DR PDB; 6HIP; X-ray; 1.20 A; A/B=301-401.
DR PDBsum; 2PE8; -.
DR PDBsum; 2PEH; -.
DR PDBsum; 5LSO; -.
DR PDBsum; 6HIP; -.
DR AlphaFoldDB; Q96I25; -.
DR BMRB; Q96I25; -.
DR SMR; Q96I25; -.
DR BioGRID; 124416; 153.
DR CORUM; Q96I25; -.
DR DIP; DIP-29409N; -.
DR IntAct; Q96I25; 65.
DR MINT; Q96I25; -.
DR STRING; 9606.ENSP00000388638; -.
DR BindingDB; Q96I25; -.
DR ChEMBL; CHEMBL4680038; -.
DR GlyGen; Q96I25; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96I25; -.
DR MetOSite; Q96I25; -.
DR PhosphoSitePlus; Q96I25; -.
DR SwissPalm; Q96I25; -.
DR BioMuta; RBM17; -.
DR DMDM; 34925383; -.
DR EPD; Q96I25; -.
DR jPOST; Q96I25; -.
DR MassIVE; Q96I25; -.
DR MaxQB; Q96I25; -.
DR PaxDb; Q96I25; -.
DR PeptideAtlas; Q96I25; -.
DR PRIDE; Q96I25; -.
DR ProteomicsDB; 76807; -.
DR ABCD; Q96I25; 1 sequenced antibody.
DR Antibodypedia; 43907; 130 antibodies from 25 providers.
DR DNASU; 84991; -.
DR Ensembl; ENST00000379888.9; ENSP00000369218.4; ENSG00000134453.16.
DR Ensembl; ENST00000446108.5; ENSP00000388638.1; ENSG00000134453.16.
DR GeneID; 84991; -.
DR KEGG; hsa:84991; -.
DR MANE-Select; ENST00000379888.9; ENSP00000369218.4; NM_032905.5; NP_116294.1.
DR UCSC; uc001ijb.4; human.
DR CTD; 84991; -.
DR DisGeNET; 84991; -.
DR GeneCards; RBM17; -.
DR HGNC; HGNC:16944; RBM17.
DR HPA; ENSG00000134453; Low tissue specificity.
DR MIM; 606935; gene.
DR neXtProt; NX_Q96I25; -.
DR OpenTargets; ENSG00000134453; -.
DR PharmGKB; PA134860993; -.
DR VEuPathDB; HostDB:ENSG00000134453; -.
DR eggNOG; KOG1996; Eukaryota.
DR GeneTree; ENSGT00790000123099; -.
DR HOGENOM; CLU_044888_0_0_1; -.
DR InParanoid; Q96I25; -.
DR OMA; EERFGNN; -.
DR OrthoDB; 1101846at2759; -.
DR PhylomeDB; Q96I25; -.
DR TreeFam; TF313987; -.
DR PathwayCommons; Q96I25; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q96I25; -.
DR SIGNOR; Q96I25; -.
DR BioGRID-ORCS; 84991; 782 hits in 1079 CRISPR screens.
DR ChiTaRS; RBM17; human.
DR EvolutionaryTrace; Q96I25; -.
DR GeneWiki; RBM17; -.
DR GenomeRNAi; 84991; -.
DR Pharos; Q96I25; Tbio.
DR PRO; PR:Q96I25; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q96I25; protein.
DR Bgee; ENSG00000134453; Expressed in metanephros cortex and 183 other tissues.
DR ExpressionAtlas; Q96I25; baseline and differential.
DR Genevisible; Q96I25; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IMP: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 CDD; cd12647; RRM_UHM_SPF45; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00221; -.
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 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Spliceosome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..401
FT /note="Splicing factor 45"
FT /id="PRO_0000081903"
FT DOMAIN 235..283
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 306..385
FT /note="RRM"
FT REGION 57..84
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:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 41
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8JZX4"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 41
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 319
FT /note="D->A: Impairs interaction with SF1; has minor effect
FT on interaction with SF3B1 and U2AF2."
FT /evidence="ECO:0000269|PubMed:17589525"
FT MUTAGEN 319
FT /note="D->K: Abolishes interaction with SF3B1, SF1 and
FT U2AF2. Abolishes regulation of alternative splicing."
FT /evidence="ECO:0000269|PubMed:17589525"
FT MUTAGEN 375
FT /note="R->A: Impairs interaction with SF3B1, SF1 and U2AF2.
FT Abolishes regulation of alternative splicing."
FT /evidence="ECO:0000269|PubMed:17589525"
FT MUTAGEN 376
FT /note="Y->A: Impairs interaction with SF3B1, SF1 and U2AF2.
FT Abolishes regulation of alternative splicing."
FT /evidence="ECO:0000269|PubMed:17589525"
FT MUTAGEN 377
FT /note="F->A: Impairs interaction with SF1 and U2AF2 and
FT abolishes interaction with SF3B1. Abolishes regulation of
FT alternative splicing."
FT /evidence="ECO:0000269|PubMed:17589525"
FT CONFLICT 214
FT /note="Y -> H (in Ref. 1; AAH09064)"
FT /evidence="ECO:0000305"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:6HIP"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:6HIP"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:6HIP"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:6HIP"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:6HIP"
FT STRAND 352..361
FT /evidence="ECO:0007829|PDB:6HIP"
FT HELIX 362..372
FT /evidence="ECO:0007829|PDB:6HIP"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:6HIP"
FT HELIX 389..393
FT /evidence="ECO:0007829|PDB:6HIP"
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
