SLU7_HUMAN
ID SLU7_HUMAN Reviewed; 586 AA.
AC O95391; D3DQK2; Q3LUJ0; Q3LUJ1; Q6RXQ5; Q96FM9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Pre-mRNA-splicing factor SLU7;
DE Short=hSlu7;
GN Name=SLU7;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH LATE SPLICEOSOMAL COMPLEX, AND VARIANT THR-229.
RX PubMed=10197984; DOI=10.1101/gad.13.7.841;
RA Chua K., Reed R.;
RT "Human step II splicing factor hSlu7 functions in restructuring the
RT spliceosome between the catalytic steps of splicing.";
RL Genes Dev. 13:841-850(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-229.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-111 AND THR-229.
RC TISSUE=Eye;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-102.
RC TISSUE=Colon;
RA Holste D., Shomron N., Burge C.B.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION.
RX PubMed=10647016; DOI=10.1038/46086;
RA Chua K., Reed R.;
RT "The RNA splicing factor hSlu7 is required for correct 3' splice-site
RT choice.";
RL Nature 402:207-210(1999).
RN [7]
RP FUNCTION.
RX PubMed=12764196; DOI=10.1126/science.1082588;
RA Lev-Maor G., Sorek R., Shomron N., Ast G.;
RT "The birth of an alternatively spliced exon: 3' splice-site selection in
RT Alu exons.";
RL Science 300:1288-1291(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN CCHC-TYPE ZINC-FINGER, ZINC-BINDING,
RP AND MUTAGENESIS OF ARG-116; LYS-117; CYS-120; CYS-123; 125-ALA-MET-126;
RP HIS-128; LYS-129; CYS-133 AND LYS-166.
RX PubMed=15181151; DOI=10.1091/mbc.e04-02-0152;
RA Shomron N., Reznik M., Ast G.;
RT "Splicing factor hSlu7 contains a unique functional domain required to
RT retain the protein within the nucleus.";
RL Mol. Biol. Cell 15:3782-3795(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15728250; DOI=10.1242/jcs.01720;
RA Shomron N., Alberstein M., Reznik M., Ast G.;
RT "Stress alters the subcellular distribution of hSlu7 and thus modulates
RT alternative splicing.";
RL J. Cell Sci. 118:1151-1159(2005).
RN [10]
RP ERRATUM OF PUBMED:15728250.
RA Shomron N., Alberstein M., Reznik M., Ast G.;
RL J. Cell Sci. 118:1331-1331(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, VARIANT [LARGE SCALE
RP ANALYSIS] THR-229, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
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=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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-227 AND SER-235,
RP VARIANT [LARGE SCALE ANALYSIS] THR-229, AND IDENTIFICATION BY MASS
RP 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 [16]
RP SUBCELLULAR LOCATION.
RX PubMed=21122810; DOI=10.1016/j.bbamcr.2010.11.010;
RA Janowicz A., Michalak M., Krebs J.;
RT "Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7.";
RL Biochim. Biophys. Acta 1813:1045-1049(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-235, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-227 AND SER-235,
RP VARIANT [LARGE SCALE ANALYSIS] THR-229, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-235, 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 [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-349 AND LYS-408, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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 [21] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [22] {ECO:0007744|PDB:6QDV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=30705154; DOI=10.1126/science.aaw5569;
RA Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.;
RT "A human postcatalytic spliceosome structure reveals essential roles of
RT metazoan factors for exon ligation.";
RL Science 363:710-714(2019).
CC -!- FUNCTION: Required for pre-mRNA splicing as component of the
CC spliceosome (PubMed:10197984, PubMed:28502770, PubMed:30705154).
CC Participates in the second catalytic step of pre-mRNA splicing, when
CC the free hydroxyl group of exon I attacks the 3'-splice site to
CC generate spliced mRNA and the excised lariat intron. Required for
CC holding exon 1 properly in the spliceosome and for correct AG
CC identification when more than one possible AG exists in 3'-splicing
CC site region. May be involved in the activation of proximal AG. Probably
CC also involved in alternative splicing regulation.
CC {ECO:0000269|PubMed:10197984, ECO:0000269|PubMed:10647016,
CC ECO:0000269|PubMed:12764196, ECO:0000269|PubMed:15181151,
CC ECO:0000269|PubMed:15728250, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:30705154}.
CC -!- SUBUNIT: Component of pre-catalytic, catalytic and post-catalytic
CC spliceosomes (PubMed:10197984, PubMed:28502770, PubMed:30705154).
CC Associates with the spliceosome prior to recognition of the 3'-splice
CC site for step II, probably during catalysis of step I
CC (PubMed:10197984). {ECO:0000269|PubMed:10197984,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:30705154}.
CC -!- INTERACTION:
CC O95391; Q13155: AIMP2; NbExp=3; IntAct=EBI-750559, EBI-745226;
CC O95391; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-750559, EBI-702390;
CC O95391; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-750559, EBI-739624;
CC O95391; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-750559, EBI-745369;
CC O95391; Q13643: FHL3; NbExp=3; IntAct=EBI-750559, EBI-741101;
CC O95391; P14136: GFAP; NbExp=3; IntAct=EBI-750559, EBI-744302;
CC O95391; Q08379: GOLGA2; NbExp=6; IntAct=EBI-750559, EBI-618309;
CC O95391; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-750559, EBI-81279;
CC O95391; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-750559, EBI-1055254;
CC O95391; Q6A162: KRT40; NbExp=3; IntAct=EBI-750559, EBI-10171697;
CC O95391; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-750559, EBI-2341787;
CC O95391; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-750559, EBI-741037;
CC O95391; P23508: MCC; NbExp=3; IntAct=EBI-750559, EBI-307531;
CC O95391; P19404: NDUFV2; NbExp=3; IntAct=EBI-750559, EBI-713665;
CC O95391; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-750559, EBI-10271199;
CC O95391; Q9BZ95: NSD3; NbExp=2; IntAct=EBI-750559, EBI-3390132;
CC O95391; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-750559, EBI-14066006;
CC O95391; Q9H2H8: PPIL3; NbExp=5; IntAct=EBI-750559, EBI-751051;
CC O95391; O43395: PRPF3; NbExp=2; IntAct=EBI-750559, EBI-744322;
CC O95391; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-750559, EBI-538479;
CC O95391; Q13435: SF3B2; NbExp=2; IntAct=EBI-750559, EBI-749111;
CC O95391; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-750559, EBI-11139477;
CC O95391; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-750559, EBI-741515;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10197984,
CC ECO:0000269|PubMed:15728250, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:30705154}. Nucleus speckle
CC {ECO:0000269|PubMed:15181151}. Cytoplasm {ECO:0000269|PubMed:15728250}.
CC Note=Predominantly nuclear. Shuttling between the nucleus and the
CC cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress
CC stimulus, the nuclear concentration of the protein decreases, affecting
CC alternative splicing. Translocates from the nucleus to the cytoplasm
CC after heat shock cell treatment. Accumulates in cytoplasmic vesicle-
CC like organelles after heat shock treatment, which may represent stress
CC granules. {ECO:0000269|PubMed:15728250}.
CC -!- DOMAIN: The CCHC-type zinc finger is required to retain the protein
CC within the nucleus and prevent its shuttle back to the cytoplasm via
CC the CRM1 pathway. {ECO:0000269|PubMed:15181151}.
CC -!- SIMILARITY: Belongs to the SLU7 family. {ECO:0000305}.
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DR EMBL; AF101074; AAD13774.1; -; mRNA.
DR EMBL; AC091842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61554.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61555.1; -; Genomic_DNA.
DR EMBL; BC010634; AAH10634.1; -; mRNA.
DR EMBL; AY486334; AAS59410.1; -; mRNA.
DR EMBL; DQ174516; ABA08382.1; -; mRNA.
DR EMBL; DQ174517; ABA08383.1; -; mRNA.
DR CCDS; CCDS4352.1; -.
DR RefSeq; NP_006416.3; NM_006425.4.
DR RefSeq; XP_011532720.1; XM_011534418.2.
DR PDB; 5XJC; EM; 3.60 A; Z=1-586.
DR PDB; 6ICZ; EM; 3.00 A; Z=1-586.
DR PDB; 6QDV; EM; 3.30 A; c=1-586.
DR PDBsum; 5XJC; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6QDV; -.
DR AlphaFoldDB; O95391; -.
DR SMR; O95391; -.
DR BioGRID; 115820; 113.
DR CORUM; O95391; -.
DR IntAct; O95391; 53.
DR MINT; O95391; -.
DR STRING; 9606.ENSP00000297151; -.
DR iPTMnet; O95391; -.
DR PhosphoSitePlus; O95391; -.
DR BioMuta; SLU7; -.
DR EPD; O95391; -.
DR jPOST; O95391; -.
DR MassIVE; O95391; -.
DR MaxQB; O95391; -.
DR PaxDb; O95391; -.
DR PeptideAtlas; O95391; -.
DR PRIDE; O95391; -.
DR ProteomicsDB; 50843; -.
DR Antibodypedia; 28531; 339 antibodies from 29 providers.
DR DNASU; 10569; -.
DR Ensembl; ENST00000297151.9; ENSP00000297151.4; ENSG00000164609.10.
DR GeneID; 10569; -.
DR KEGG; hsa:10569; -.
DR MANE-Select; ENST00000297151.9; ENSP00000297151.4; NM_006425.5; NP_006416.3.
DR UCSC; uc003lyg.4; human.
DR CTD; 10569; -.
DR DisGeNET; 10569; -.
DR GeneCards; SLU7; -.
DR HGNC; HGNC:16939; SLU7.
DR HPA; ENSG00000164609; Low tissue specificity.
DR MIM; 605974; gene.
DR neXtProt; NX_O95391; -.
DR OpenTargets; ENSG00000164609; -.
DR PharmGKB; PA128394574; -.
DR VEuPathDB; HostDB:ENSG00000164609; -.
DR eggNOG; KOG2560; Eukaryota.
DR GeneTree; ENSGT00390000002292; -.
DR HOGENOM; CLU_019317_2_0_1; -.
DR InParanoid; O95391; -.
DR OMA; KKPFYVD; -.
DR OrthoDB; 816947at2759; -.
DR PhylomeDB; O95391; -.
DR TreeFam; TF105691; -.
DR PathwayCommons; O95391; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; O95391; -.
DR BioGRID-ORCS; 10569; 747 hits in 1083 CRISPR screens.
DR ChiTaRS; SLU7; human.
DR GeneWiki; SLU7; -.
DR GenomeRNAi; 10569; -.
DR Pharos; O95391; Tbio.
DR PRO; PR:O95391; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O95391; protein.
DR Bgee; ENSG00000164609; Expressed in epithelial cell of pancreas and 189 other tissues.
DR ExpressionAtlas; O95391; baseline and differential.
DR Genevisible; O95391; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HGNC-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:HGNC-UCL.
DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IDA:HGNC-UCL.
DR GO; GO:0000386; F:second spliceosomal transesterification activity; IDA:HGNC-UCL.
DR GO; GO:0008270; F:zinc ion binding; IDA:HGNC-UCL.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:HGNC-UCL.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0000389; P:mRNA 3'-splice site recognition; IDA:HGNC-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; IDA:HGNC-UCL.
DR InterPro; IPR021715; Slu7_dom.
DR InterPro; IPR039974; Splicing_factor_SLU7.
DR PANTHER; PTHR12942; PTHR12942; 1.
DR Pfam; PF11708; Slu7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Isopeptide bond; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..586
FT /note="Pre-mRNA-splicing factor SLU7"
FT /id="PRO_0000289194"
FT ZN_FING 118..135
FT /note="CCHC-type"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 129..169
FT /note="Bipartite nuclear localization signal"
FT COMPBIAS 20..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..577
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 MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 111
FT /note="I -> V (in dbSNP:rs17856338)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_032598"
FT VARIANT 229
FT /note="M -> T (in dbSNP:rs2961944)"
FT /evidence="ECO:0000269|PubMed:10197984,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_032599"
FT MUTAGEN 116
FT /note="R->N: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 117
FT /note="K->N: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 120
FT /note="C->S: Induces a cytoplasmic localization; when
FT associated with S-123; G-128 and S-133."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 123
FT /note="C->S: Induces a cytoplasmic localization; when
FT associated with S-120; G-128 and S-133."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 125..126
FT /note="AM->VP: Does not affect nuclear localization."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 128
FT /note="H->G: Induces a cytoplasmic localization; when
FT associated with S-120; S-123 and S-133."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 129
FT /note="K->N: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 133
FT /note="C->S: Induces a cytoplasmic localization; when
FT associated with S-120; S-123 and G-128."
FT /evidence="ECO:0000269|PubMed:15181151"
FT MUTAGEN 136
FT /note="R->N: Abolishes nuclear localization."
FT MUTAGEN 166
FT /note="K->N: Abolishes nuclear localization."
FT /evidence="ECO:0000269|PubMed:15181151"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 169..172
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 287..290
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:6ICZ"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 320..337
FT /evidence="ECO:0007829|PDB:6ICZ"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:6ICZ"
FT HELIX 347..368
FT /evidence="ECO:0007829|PDB:6ICZ"
SQ SEQUENCE 586 AA; 68387 MW; 237B8C8014EEAB6E CRC64;
MSATVVDAVN AAPLSGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN
PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE WYKRGVKENS IITKYRKGAC
ENCGAMTHKK KDCFERPRRV GAKFTGTNIA PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK
IVEEYAKVDL AKRTLKAQKL QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE
DKYADDIDMP GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA
GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL ELLYKSFKVK
KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY SRHGTVIKGQ ERAVACSKYE
EDVKIHNHTH IWGSYWKEGR WGYKCCHSFF KYSYCTGEAG KEIVNSEECI INEITGEESV
KKPQTLMELH QEKLKEEKKK KKKKKKKHRK SSSDSDDEEK KHEKLKKALN AEEARLLHVK
ETMQIDERKR PYNSMYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ
