SRRM1_HUMAN
ID SRRM1_HUMAN Reviewed; 904 AA.
AC Q8IYB3; O60585; Q5VVN4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Serine/arginine repetitive matrix protein 1;
DE AltName: Full=SR-related nuclear matrix protein of 160 kDa;
DE Short=SRm160;
DE AltName: Full=Ser/Arg-related nuclear matrix protein;
GN Name=SRRM1; Synonyms=SRM160;
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] (ISOFORM 2), FUNCTION IN MRNA SPLICING,
RP IDENTIFICATION IN A PRE-MRNA SPLICING COMPLEX WITH SFRS4; SFRS5; SNRP70;
RP SNRPA1 AND SRRM2, AND SUBCELLULAR LOCATION.
RX PubMed=9531537; DOI=10.1101/gad.12.7.996;
RA Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.;
RT "A coactivator of pre-mRNA splicing.";
RL Genes Dev. 12:996-1009(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Guo J.H., Yu L.;
RT "Molecular cloning and characterization of human SRM160 gene.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-170.
RC TISSUE=Testis;
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 PROTEIN SEQUENCE OF 1-7; 30-36; 43-54; 84-96; 230-246; 387-396; 690-701 AND
RP 870-885, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-389 AND SER-393, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma, and Ovarian carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Lilla S.,
RA von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP FUNCTION IN MRNA EXONIC SPLICING ENHANCER (ESE)-DEPENDENT SPLICING, AND
RP IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX WITH
RP SNRP70; SNRPA1 AND TRA2B.
RX PubMed=10339552; DOI=10.1073/pnas.96.11.6125;
RA Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.;
RT "The SRm160/300 splicing coactivator is required for exon-enhancer
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999).
RN [7]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC)
RP WITH DEK; RBM8A; RNPS1 AND ALYREF/THOC4.
RX PubMed=11118221; DOI=10.1093/emboj/19.24.6860;
RA Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.;
RT "The spliceosome deposits multiple proteins 20-24 nucleotides upstream of
RT mRNA exon-exon junctions.";
RL EMBO J. 19:6860-6869(2000).
RN [8]
RP IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX (EJC)
RP WITH PRPF8, ASSOCIATION WITH THE SPLICEOSOME, AND RNA-BINDING.
RX PubMed=10809668;
RA Le Hir H., Moore M.J., Maquat L.E.;
RT "Pre-mRNA splicing alters mRNP composition: evidence for stable association
RT of proteins at exon-exon junctions.";
RL Genes Dev. 14:1098-1108(2000).
RN [9]
RP FUNCTION IN MRNA SPLICING.
RX PubMed=10668804; DOI=10.1017/s1355838200991982;
RA Blencowe B.J., Bauren G., Eldridge A.G., Issner R., Nickerson J.A.,
RA Rosonina E., Sharp P.A.;
RT "The SRm160/300 splicing coactivator subunits.";
RL RNA 6:111-120(2000).
RN [10]
RP RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11546874; DOI=10.1126/science.1062786;
RA Lykke-Andersen J., Shu M.-D., Steitz J.A.;
RT "Communication of the position of exon-exon junctions to the mRNA
RT surveillance machinery by the protein RNPS1.";
RL Science 293:1836-1839(2001).
RN [11]
RP INTERACTION WITH THE EXON JUNCTION COMPLEX.
RX PubMed=12093754; DOI=10.1093/emboj/cdf345;
RA Lejeune F., Ishigaki Y., Li X., Maquat L.E.;
RT "The exon junction complex is detected on CBP80-bound but not eIF4E-bound
RT mRNA in mammalian cells: dynamics of mRNP remodeling.";
RL EMBO J. 21:3536-3545(2002).
RN [12]
RP FUNCTION IN MRNA SPLICING AND 3'-END FORMATION, AND INTERACTION WITH CPSF1.
RX PubMed=11739730; DOI=10.1128/mcb.22.1.148-160.2002;
RA McCracken S., Lambermon M., Blencowe B.J.;
RT "SRm160 splicing coactivator promotes transcript 3'-end cleavage.";
RL Mol. Cell. Biol. 22:148-160(2002).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [14]
RP FUNCTION IN MRNA 3'-END FORMATION, AND INTERACTION WITH DDX39B; RBM8A;
RP RNPS1 AND ALYREF/THOC4.
RX PubMed=12944400; DOI=10.1074/jbc.m306856200;
RA McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
RT "An evolutionarily conserved role for SRm160 in 3'-end processing that
RT functions independently of exon junction complex formation.";
RL J. Biol. Chem. 278:44153-44160(2003).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=12624182; DOI=10.1073/pnas.0438055100;
RA Wagner S., Chiosea S., Nickerson J.A.;
RT "The spatial targeting and nuclear matrix binding domains of SRm160.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:3269-3274(2003).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402 AND THR-406, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [17]
RP ATP-DEPENDENT MOBILITY OF A SRRM1-COMPLEX.
RX PubMed=15024032; DOI=10.1083/jcb.200307002;
RA Wagner S., Chiosea S., Ivshina M., Nickerson J.A.;
RT "In vitro FRAP reveals the ATP-dependent nuclear mobilization of the exon
RT junction complex protein SRm160.";
RL J. Cell Biol. 164:843-850(2004).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-260; SER-402;
RP THR-406; SER-450; SER-452; SER-463; SER-465; SER-560; SER-562; THR-614;
RP SER-616; SER-626; SER-628; THR-872 AND SER-874, AND IDENTIFICATION BY MASS
RP 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-560; SER-562;
RP THR-614; SER-616; SER-754 AND SER-756, AND IDENTIFICATION BY MASS
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-429; SER-431;
RP SER-436; SER-597; SER-605; SER-607; SER-694; SER-696; SER-713; SER-715;
RP SER-748; SER-752; SER-754; SER-756; SER-769; SER-775; SER-777 AND SER-781,
RP AND 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-872 AND SER-874, AND
RP IDENTIFICATION BY 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 [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-738; SER-740;
RP SER-769; SER-775; SER-781; THR-872 AND SER-874, AND IDENTIFICATION BY MASS
RP 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 [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-140, 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-227; SER-234;
RP SER-260; SER-389; SER-391; SER-393; SER-402; THR-406; SER-429; SER-431;
RP SER-450; SER-452; SER-463; SER-465; SER-478; SER-560; SER-562; SER-597;
RP SER-605; SER-607; THR-614; SER-616; SER-626; SER-628; SER-636; SER-638;
RP SER-696; SER-738; SER-752; SER-754; SER-756; SER-769; SER-781; THR-872 AND
RP SER-874, AND 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 [28]
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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-260; SER-389;
RP SER-391; SER-393; SER-402; SER-414; THR-416; SER-420; SER-429; SER-431;
RP SER-450; SER-452; SER-463; SER-465; SER-549; SER-551; THR-555; THR-572;
RP THR-574; THR-581; SER-583; SER-597; SER-605; SER-607; SER-616; SER-626;
RP SER-628; SER-636; SER-638; SER-696; SER-705; SER-707; SER-738; SER-740;
RP SER-754; SER-756; SER-769; SER-791; THR-793; SER-795; THR-872 AND SER-874,
RP AND 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 [30]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-234; SER-240;
RP THR-241; SER-260; SER-389; SER-391; SER-393; SER-429; SER-431; SER-450;
RP SER-452; SER-463; SER-465; SER-560; SER-562; SER-605; SER-607; THR-614;
RP SER-616; SER-694; SER-696; SER-713; SER-715; SER-738; SER-740; SER-748;
RP SER-752; SER-754; SER-756; SER-769; SER-775; SER-781; SER-791; SER-797;
RP SER-802; THR-872 AND SER-874, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-234; SER-260;
RP SER-389; SER-402; THR-406; SER-450; SER-524; SER-526; SER-528; SER-530;
RP SER-532; SER-549; SER-551; SER-560; SER-562; TYR-596; SER-597; THR-614;
RP SER-616; SER-638; SER-705; SER-713; THR-718; SER-738; SER-769; SER-773;
RP SER-781; SER-874 AND SER-901, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-231, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-231; LYS-249; LYS-447;
RP LYS-459; LYS-472 AND LYS-869, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [37]
RP PHOSPHORYLATION.
RX PubMed=29973724; DOI=10.1038/s41586-018-0279-8;
RA Rai A.K., Chen J.X., Selbach M., Pelkmans L.;
RT "Kinase-controlled phase transition of membraneless organelles in
RT mitosis.";
RL Nature 559:211-216(2018).
RN [38]
RP STRUCTURE BY NMR OF 27-134, FUNCTION IN MRNA 3'-END FORMATION, MUTAGENESIS
RP OF LYS-20; LYS-22 AND LYS-23, DNA-BINDING, AND RNA-BINDING.
RX PubMed=12600940; DOI=10.1101/gad.1060403;
RA Szymczyna B.R., Bowman J., McCracken S., Pineda-Lucena A., Lu Y., Cox B.,
RA Lambermon M., Graveley B.R., Arrowsmith C.H., Blencowe B.J.;
RT "Structure and function of the PWI motif: a novel nucleic acid-binding
RT domain that facilitates pre-mRNA processing.";
RL Genes Dev. 17:461-475(2003).
CC -!- FUNCTION: Part of pre- and post-splicing multiprotein mRNP complexes.
CC Involved in numerous pre-mRNA processing events. Promotes constitutive
CC and exonic splicing enhancer (ESE)-dependent splicing activation by
CC bridging together sequence-specific (SR family proteins, SFRS4, SFRS5
CC and TRA2B/SFRS10) and basal snRNP (SNRP70 and SNRPA1) factors of the
CC spliceosome. Stimulates mRNA 3'-end cleavage independently of the
CC formation of an exon junction complex. Binds both pre-mRNA and spliced
CC mRNA 20-25 nt upstream of exon-exon junctions. Binds RNA and DNA with
CC low sequence specificity and has similar preference for either
CC double- or single-stranded nucleic acid substrates.
CC {ECO:0000269|PubMed:10339552, ECO:0000269|PubMed:10668804,
CC ECO:0000269|PubMed:11739730, ECO:0000269|PubMed:12600940,
CC ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:9531537}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Found in a pre-mRNA
CC splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and SRRM2.
CC Found in a pre-mRNA exonic splicing enhancer (ESE) complex with SNRP70,
CC SNRPA1, SRRM1 and TRA2B/SFRS10. Found in a mRNA splicing-dependent exon
CC junction complex (EJC) with DEK, PRPF8, NCBP1, RBM8A, RNPS1, SRRM1 and
CC ALYREF/THOC4. Interacts with DDX39B, CPSF1, RBM8A, RNPS1, and
CC ALYREF/THOC4. Seems to be a compound of RNA export complexes that are
CC released from speckles in a ATP-dependent manner.
CC {ECO:0000269|PubMed:10339552, ECO:0000269|PubMed:10809668,
CC ECO:0000269|PubMed:11118221, ECO:0000269|PubMed:11739730,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12093754,
CC ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:9531537}.
CC -!- INTERACTION:
CC Q8IYB3; P49760: CLK2; NbExp=6; IntAct=EBI-1055880, EBI-750020;
CC Q8IYB3; P49760-3: CLK2; NbExp=3; IntAct=EBI-1055880, EBI-11535445;
CC Q8IYB3; P78362: SRPK2; NbExp=3; IntAct=EBI-1055880, EBI-593303;
CC Q8IYB3; A7MD48: SRRM4; NbExp=3; IntAct=EBI-1055880, EBI-3867173;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:12624182,
CC ECO:0000269|PubMed:9531537}. Nucleus speckle
CC {ECO:0000269|PubMed:11546874, ECO:0000269|PubMed:9531537}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IYB3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IYB3-2; Sequence=VSP_016522, VSP_016523;
CC -!- PTM: Phosphorylated on multiple serine and threonine residues by DYRK3
CC during the G2-to-M transition, after the nuclear-envelope breakdown
CC (PubMed:29973724). Phosphorylation by DYRK3 promotes disassembly of
CC nuclear speckles (PubMed:29973724). {ECO:0000269|PubMed:29973724}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q52KI8}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC09321.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP97290.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF048977; AAC09321.1; ALT_FRAME; mRNA.
DR EMBL; AF419855; AAP97290.1; ALT_FRAME; mRNA.
DR EMBL; AL445648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036187; AAH36187.1; -; mRNA.
DR CCDS; CCDS255.1; -. [Q8IYB3-1]
DR RefSeq; NP_001290377.1; NM_001303448.1.
DR RefSeq; NP_001290378.1; NM_001303449.1.
DR RefSeq; NP_005830.2; NM_005839.3. [Q8IYB3-1]
DR PDB; 1MP1; NMR; -; A=27-134.
DR PDB; 6FF4; EM; 16.00 A; Y=1-904.
DR PDB; 6FF7; EM; 4.50 A; Y=1-904.
DR PDB; 7ABG; EM; 7.80 A; Y=1-904.
DR PDB; 7ABH; EM; 4.50 A; Y=1-904.
DR PDB; 7ABI; EM; 8.00 A; Y=1-904.
DR PDB; 7DVQ; EM; 2.89 A; 8=1-904.
DR PDBsum; 1MP1; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABH; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; Q8IYB3; -.
DR BMRB; Q8IYB3; -.
DR SMR; Q8IYB3; -.
DR BioGRID; 115544; 265.
DR CORUM; Q8IYB3; -.
DR IntAct; Q8IYB3; 60.
DR MINT; Q8IYB3; -.
DR STRING; 9606.ENSP00000326261; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR CarbonylDB; Q8IYB3; -.
DR GlyGen; Q8IYB3; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q8IYB3; -.
DR PhosphoSitePlus; Q8IYB3; -.
DR SwissPalm; Q8IYB3; -.
DR BioMuta; SRRM1; -.
DR DMDM; 83305833; -.
DR EPD; Q8IYB3; -.
DR jPOST; Q8IYB3; -.
DR MassIVE; Q8IYB3; -.
DR MaxQB; Q8IYB3; -.
DR PaxDb; Q8IYB3; -.
DR PeptideAtlas; Q8IYB3; -.
DR PRIDE; Q8IYB3; -.
DR ProteomicsDB; 71140; -. [Q8IYB3-1]
DR ProteomicsDB; 71141; -. [Q8IYB3-2]
DR Antibodypedia; 30330; 124 antibodies from 22 providers.
DR DNASU; 10250; -.
DR Ensembl; ENST00000323848.14; ENSP00000326261.8; ENSG00000133226.18. [Q8IYB3-1]
DR GeneID; 10250; -.
DR KEGG; hsa:10250; -.
DR MANE-Select; ENST00000323848.14; ENSP00000326261.8; NM_005839.4; NP_005830.2.
DR UCSC; uc001bjm.4; human. [Q8IYB3-1]
DR CTD; 10250; -.
DR DisGeNET; 10250; -.
DR GeneCards; SRRM1; -.
DR HGNC; HGNC:16638; SRRM1.
DR HPA; ENSG00000133226; Low tissue specificity.
DR MIM; 605975; gene.
DR neXtProt; NX_Q8IYB3; -.
DR OpenTargets; ENSG00000133226; -.
DR PharmGKB; PA38177; -.
DR VEuPathDB; HostDB:ENSG00000133226; -.
DR eggNOG; KOG2146; Eukaryota.
DR GeneTree; ENSGT00730000111080; -.
DR HOGENOM; CLU_015415_0_0_1; -.
DR InParanoid; Q8IYB3; -.
DR OrthoDB; 1210775at2759; -.
DR PhylomeDB; Q8IYB3; -.
DR TreeFam; TF318972; -.
DR PathwayCommons; Q8IYB3; -.
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 Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9013422; RHOBTB1 GTPase cycle.
DR SignaLink; Q8IYB3; -.
DR BioGRID-ORCS; 10250; 614 hits in 1083 CRISPR screens.
DR ChiTaRS; SRRM1; human.
DR EvolutionaryTrace; Q8IYB3; -.
DR GeneWiki; SRRM1; -.
DR GenomeRNAi; 10250; -.
DR Pharos; Q8IYB3; Tbio.
DR PRO; PR:Q8IYB3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IYB3; protein.
DR Bgee; ENSG00000133226; Expressed in corpus epididymis and 206 other tissues.
DR ExpressionAtlas; Q8IYB3; baseline and differential.
DR Genevisible; Q8IYB3; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR DisProt; DP02359; -.
DR InterPro; IPR002483; PWI_dom.
DR InterPro; IPR036483; PWI_dom_sf.
DR Pfam; PF01480; PWI; 1.
DR SMART; SM00311; PWI; 1.
DR SUPFAM; SSF101233; SSF101233; 1.
DR PROSITE; PS51025; PWI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Citrullination;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..904
FT /note="Serine/arginine repetitive matrix protein 1"
FT /id="PRO_0000076326"
FT DOMAIN 27..126
FT /note="PWI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00627"
FT REGION 1..156
FT /note="Necessary for mRNA 3'-end cleavage and cytoplasmic
FT accumulation"
FT REGION 1..151
FT /note="Necessary for DNA and RNA-binding"
FT REGION 139..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..688
FT /note="Necessary for speckles and matrix localization"
FT COMPBIAS 139..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..349
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..593
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..636
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..835
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22814378"
FT MOD_RES 7
FT /note="Citrulline"
FT /evidence="ECO:0000250"
FT MOD_RES 140
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19367720,
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 MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 572
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 581
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 596
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 614
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52KI8"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 705
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 718
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="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 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 773
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 777
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 778
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q52KI8"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 793
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 802
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 872
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, 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 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 127
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 869
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 305..308
FT /note="RSRS -> DKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9531537, ECO:0000303|Ref.2"
FT /id="VSP_016522"
FT VAR_SEQ 407
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9531537, ECO:0000303|Ref.2"
FT /id="VSP_016523"
FT VARIANT 170
FT /note="R -> H (in dbSNP:rs17857102)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024065"
FT MUTAGEN 20
FT /note="K->A: Strongly reduces DNA and RNA-binding."
FT /evidence="ECO:0000269|PubMed:12600940"
FT MUTAGEN 22
FT /note="K->A: Strongly reduces DNA and RNA-binding."
FT /evidence="ECO:0000269|PubMed:12600940"
FT MUTAGEN 23
FT /note="K->A: Strongly reduces DNA and RNA-binding."
FT /evidence="ECO:0000269|PubMed:12600940"
FT CONFLICT 269
FT /note="K -> Q (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="R -> Q (in Ref. 4; AAH36187)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="H -> D (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT TURN 11..13
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:6FF4"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 904 AA; 102335 MW; 27D4D2A48EDBFED3 CRC64;
MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP WITKRVTEIL
GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE FMGELWPLLL SAQENIAGIP
SAFLELKKEE IKQRQIEQEK LASMKKQDED KDKRDKEEKE SSREKRERSR SPRRRKSRSP
SPRRRSSPVR RERKRSHSRS PRHRTKSRSP SPAPEKKEKT PELPEPSVKV KEPSVQEATS
TSDILKVPKP EPIPEPKEPS PEKNSKKEKE KEKTRPRSRS RSKSRSRTRS RSPSHTRPRR
RHRSRSRSYS PRRRPSPRRR PSPRRRTPPR RMPPPPRHRR SRSPVRRRRR SSASLSGSSS
SSSSSRSRSP PKKPPKRTSS PPRKTRRLSP SASPPRRRHR PSPPATPPPK TRHSPTPQQS
NRTRKSRVSV SPGRTSGKVT KHKGTEKRES PSPAPKPRKV ELSESEEDKG GKMAAADSVQ
QRRQYRRQNQ QSSSDSGSSS SSEDERPKRS HVKNGEVGRR RRHSPSRSAS PSPRKRQKET
SPRGRRRRSP SPPPTRRRRS PSPAPPPRRR RTPTPPPRRR TPSPPPRRRS PSPRRYSPPI
QRRYSPSPPP KRRTASPPPP PKRRASPSPP PKRRVSHSPP PKQRSSPVTK RRSPSLSSKH
RKGSSPSRST REARSPQPNK RHSPSPRPRA PQTSSSPPPV RRGASSSPQR RQSPSPSTRP
IRRVSRTPEP KKIKKAASPS PQSVRRVSSS RSVSGSPEPA AKKPPAPPSP VQSQSPSTNW
SPAVPVKKAK SPTPSPSPPR NSDQEGGGKK KKKKKDKKHK KDKKHKKHKK HKKEKAVAAA
AAAAVTPAAI AAATTTLAQE EPVAAPEPKK ETESEAEDNL DDLEKHLREK ALRSMRKAQV
SPQS
