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Serine/arginine repetitive matrix protein 1 (SR-related nuclear matrix protein of 160 kDa) (SRm160) (Ser/Arg-related nuclear matrix protein)

 SRRM1_HUMAN             Reviewed;         904 AA.
Q8IYB3; O60585; Q5VVN4;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
23-MAY-2018, entry version 160.
RecName: Full=Serine/arginine repetitive matrix protein 1;
AltName: Full=SR-related nuclear matrix protein of 160 kDa;
Short=SRm160;
AltName: Full=Ser/Arg-related nuclear matrix protein;
Name=SRRM1; Synonyms=SRM160;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN MRNA SPLICING,
IDENTIFICATION IN A PRE-MRNA SPLICING COMPLEX WITH SFRS4; SFRS5;
SNRP70; SNRPA1 AND SRRM2, AND SUBCELLULAR LOCATION.
PubMed=9531537; DOI=10.1101/gad.12.7.996;
Blencowe B.J., Issner R., Nickerson J.A., Sharp P.A.;
"A coactivator of pre-mRNA splicing.";
Genes Dev. 12:996-1009(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Guo J.H., Yu L.;
"Molecular cloning and characterization of human SRM160 gene.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
HIS-170.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 1-7; 30-36; 43-54; 84-96; 230-246; 387-396;
690-701 AND 870-885, ACETYLATION AT MET-1, PHOSPHORYLATION AT SER-389
AND SER-393, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E., Lilla S.,
von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[6]
FUNCTION IN MRNA EXONIC SPLICING ENHANCER (ESE)-DEPENDENT SPLICING,
AND IDENTIFICATION IN A MRNA EXONIC SPLICING ENHANCER (ESE) COMPLEX
WITH SNRP70; SNRPA1 AND TRA2B.
PubMed=10339552; DOI=10.1073/pnas.96.11.6125;
Eldridge A.G., Li Y., Sharp P.A., Blencowe B.J.;
"The SRm160/300 splicing coactivator is required for exon-enhancer
function.";
Proc. Natl. Acad. Sci. U.S.A. 96:6125-6130(1999).
[7]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX
(EJC) WITH DEK; RBM8A; RNPS1 AND ALYREF/THOC4.
PubMed=11118221; DOI=10.1093/emboj/19.24.6860;
Le Hir H., Izaurralde E., Maquat L.E., Moore M.J.;
"The spliceosome deposits multiple proteins 20-24 nucleotides upstream
of mRNA exon-exon junctions.";
EMBO J. 19:6860-6869(2000).
[8]
IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX
(EJC) WITH PRPF8, ASSOCIATION WITH THE SPLICEOSOME, AND RNA-BINDING.
PubMed=10809668;
Le Hir H., Moore M.J., Maquat L.E.;
"Pre-mRNA splicing alters mRNP composition: evidence for stable
association of proteins at exon-exon junctions.";
Genes Dev. 14:1098-1108(2000).
[9]
FUNCTION IN MRNA SPLICING.
PubMed=10668804; DOI=10.1017/S1355838200991982;
Blencowe B.J., Bauren G., Eldridge A.G., Issner R., Nickerson J.A.,
Rosonina E., Sharp P.A.;
"The SRm160/300 splicing coactivator subunits.";
RNA 6:111-120(2000).
[10]
RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=11546874; DOI=10.1126/science.1062786;
Lykke-Andersen J., Shu M.-D., Steitz J.A.;
"Communication of the position of exon-exon junctions to the mRNA
surveillance machinery by the protein RNPS1.";
Science 293:1836-1839(2001).
[11]
INTERACTION WITH THE EXON JUNCTION COMPLEX.
PubMed=12093754; DOI=10.1093/emboj/cdf345;
Lejeune F., Ishigaki Y., Li X., Maquat L.E.;
"The exon junction complex is detected on CBP80-bound but not eIF4E-
bound mRNA in mammalian cells: dynamics of mRNP remodeling.";
EMBO J. 21:3536-3545(2002).
[12]
FUNCTION IN MRNA SPLICING AND 3'-END FORMATION, AND INTERACTION WITH
CPSF1.
PubMed=11739730; DOI=10.1128/MCB.22.1.148-160.2002;
McCracken S., Lambermon M., Blencowe B.J.;
"SRm160 splicing coactivator promotes transcript 3'-end cleavage.";
Mol. Cell. Biol. 22:148-160(2002).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[14]
FUNCTION IN MRNA 3'-END FORMATION, AND INTERACTION WITH BAT1; RBM8A;
RNPS1 AND ALYREF/THOC4.
PubMed=12944400; DOI=10.1074/jbc.M306856200;
McCracken S., Longman D., Johnstone I.L., Caceres J.F., Blencowe B.J.;
"An evolutionarily conserved role for SRm160 in 3'-end processing that
functions independently of exon junction complex formation.";
J. Biol. Chem. 278:44153-44160(2003).
[15]
SUBCELLULAR LOCATION.
PubMed=12624182; DOI=10.1073/pnas.0438055100;
Wagner S., Chiosea S., Nickerson J.A.;
"The spatial targeting and nuclear matrix binding domains of SRm160.";
Proc. Natl. Acad. Sci. U.S.A. 100:3269-3274(2003).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402 AND THR-406, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[17]
ATP-DEPENDENT MOBILITY OF A SRRM1-COMPLEX.
PubMed=15024032; DOI=10.1083/jcb.200307002;
Wagner S., Chiosea S., Ivshina M., Nickerson J.A.;
"In vitro FRAP reveals the ATP-dependent nuclear mobilization of the
exon junction complex protein SRm160.";
J. Cell Biol. 164:843-850(2004).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-260; SER-402;
THR-406; SER-450; SER-452; SER-463; SER-465; SER-560; SER-562;
THR-614; SER-616; SER-626; SER-628; THR-872 AND SER-874, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478; SER-560; SER-562;
THR-614; SER-616; SER-754 AND SER-756, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-452, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-429; SER-431;
SER-436; SER-597; SER-605; SER-607; SER-694; SER-696; SER-713;
SER-715; SER-748; SER-752; SER-754; SER-756; SER-769; SER-775; SER-777
AND SER-781, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-872 AND SER-874, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-738; SER-740;
SER-769; SER-775; SER-781; THR-872 AND SER-874, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-140, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-227; SER-234;
SER-260; SER-389; SER-391; SER-393; SER-402; THR-406; SER-429;
SER-431; SER-450; SER-452; SER-463; SER-465; SER-478; SER-560;
SER-562; SER-597; SER-605; SER-607; THR-614; SER-616; SER-626;
SER-628; SER-636; SER-638; SER-696; SER-738; SER-752; SER-754;
SER-756; SER-769; SER-781; THR-872 AND SER-874, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-260; SER-389;
SER-391; SER-393; SER-402; SER-414; THR-416; SER-420; SER-429;
SER-431; SER-450; SER-452; SER-463; SER-465; SER-549; SER-551;
THR-555; THR-572; THR-574; THR-581; SER-583; SER-597; SER-605;
SER-607; SER-616; SER-626; SER-628; SER-636; SER-638; SER-696;
SER-705; SER-707; SER-738; SER-740; SER-754; SER-756; SER-769;
SER-791; THR-793; SER-795; THR-872 AND SER-874, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-234; SER-240;
THR-241; SER-260; SER-389; SER-391; SER-393; SER-429; SER-431;
SER-450; SER-452; SER-463; SER-465; SER-560; SER-562; SER-605;
SER-607; THR-614; SER-616; SER-694; SER-696; SER-713; SER-715;
SER-738; SER-740; SER-748; SER-752; SER-754; SER-756; SER-769;
SER-775; SER-781; SER-791; SER-797; SER-802; THR-872 AND SER-874, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220; SER-234; SER-260;
SER-389; SER-402; THR-406; SER-450; SER-524; SER-526; SER-528;
SER-530; SER-532; SER-549; SER-551; SER-560; SER-562; TYR-596;
SER-597; THR-614; SER-616; SER-638; SER-705; SER-713; THR-718;
SER-738; SER-769; SER-773; SER-781; SER-874 AND SER-901, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-231, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-127; LYS-231; LYS-249;
LYS-447; LYS-459; LYS-472 AND LYS-869, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[37]
STRUCTURE BY NMR OF 27-134, FUNCTION IN MRNA 3'-END FORMATION,
MUTAGENESIS OF LYS-20; LYS-22 AND LYS-23, DNA-BINDING, AND
RNA-BINDING.
PubMed=12600940; DOI=10.1101/gad.1060403;
Szymczyna B.R., Bowman J., McCracken S., Pineda-Lucena A., Lu Y.,
Cox B., Lambermon M., Graveley B.R., Arrowsmith C.H., Blencowe B.J.;
"Structure and function of the PWI motif: a novel nucleic acid-binding
domain that facilitates pre-mRNA processing.";
Genes Dev. 17:461-475(2003).
-!- FUNCTION: Part of pre- and post-splicing multiprotein mRNP
complexes. Involved in numerous pre-mRNA processing events.
Promotes constitutive and exonic splicing enhancer (ESE)-dependent
splicing activation by bridging together sequence-specific (SR
family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP
(SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA
3'-end cleavage independently of the formation of an exon junction
complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of
exon-exon junctions. Binds RNA and DNA with low sequence
specificity and has similar preference for either double- or
single-stranded nucleic acid substrates.
{ECO:0000269|PubMed:10339552, ECO:0000269|PubMed:10668804,
ECO:0000269|PubMed:11739730, ECO:0000269|PubMed:12600940,
ECO:0000269|PubMed:12944400, ECO:0000269|PubMed:9531537}.
-!- SUBUNIT: Identified in the spliceosome C complex. Found in a pre-
mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and
SRRM2. Found in a pre-mRNA exonic splicing enhancer (ESE) complex
with SNRP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Found in a mRNA
splicing-dependent exon junction complex (EJC) with DEK, PRPF8,
NCBP1, RBM8A, RNPS1, SRRM1 and ALYREF/THOC4. Interacts with BAT1,
CPSF1, RBM8A, RNPS1, and ALYREF/THOC4. Seems to be a compound of
RNA export complexes that are released from speckles in a ATP-
dependent manner. {ECO:0000269|PubMed:10339552,
ECO:0000269|PubMed:10809668, ECO:0000269|PubMed:11118221,
ECO:0000269|PubMed:11739730, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12093754, ECO:0000269|PubMed:12944400,
ECO:0000269|PubMed:9531537}.
-!- INTERACTION:
P49760:CLK2; NbExp=6; IntAct=EBI-1055880, EBI-750020;
P49760-3:CLK2; NbExp=3; IntAct=EBI-1055880, EBI-11535445;
-!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus speckle.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IYB3-1; Sequence=Displayed;
Name=2;
IsoId=Q8IYB3-2; Sequence=VSP_016522, VSP_016523;
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- SIMILARITY: Belongs to the splicing factor SR family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC09321.1; Type=Frameshift; Positions=791; Evidence={ECO:0000305};
Sequence=AAP97290.1; Type=Frameshift; Positions=791; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF048977; AAC09321.1; ALT_FRAME; mRNA.
EMBL; AF419855; AAP97290.1; ALT_FRAME; mRNA.
EMBL; AL445648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL445686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC036187; AAH36187.1; -; mRNA.
CCDS; CCDS255.1; -. [Q8IYB3-1]
RefSeq; NP_001290377.1; NM_001303448.1.
RefSeq; NP_001290378.1; NM_001303449.1.
RefSeq; NP_005830.2; NM_005839.3. [Q8IYB3-1]
UniGene; Hs.18192; -.
PDB; 1MP1; NMR; -; A=27-134.
PDBsum; 1MP1; -.
ProteinModelPortal; Q8IYB3; -.
SMR; Q8IYB3; -.
BioGrid; 115544; 167.
CORUM; Q8IYB3; -.
IntAct; Q8IYB3; 26.
MINT; Q8IYB3; -.
STRING; 9606.ENSP00000326261; -.
TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
CarbonylDB; Q8IYB3; -.
iPTMnet; Q8IYB3; -.
PhosphoSitePlus; Q8IYB3; -.
SwissPalm; Q8IYB3; -.
BioMuta; SRRM1; -.
DMDM; 83305833; -.
EPD; Q8IYB3; -.
MaxQB; Q8IYB3; -.
PaxDb; Q8IYB3; -.
PeptideAtlas; Q8IYB3; -.
PRIDE; Q8IYB3; -.
Ensembl; ENST00000323848; ENSP00000326261; ENSG00000133226. [Q8IYB3-1]
GeneID; 10250; -.
KEGG; hsa:10250; -.
UCSC; uc001bjm.4; human. [Q8IYB3-1]
CTD; 10250; -.
DisGeNET; 10250; -.
EuPathDB; HostDB:ENSG00000133226.16; -.
GeneCards; SRRM1; -.
H-InvDB; HIX0023530; -.
H-InvDB; HIX0160039; -.
HGNC; HGNC:16638; SRRM1.
HPA; HPA049941; -.
HPA; HPA058612; -.
MIM; 605975; gene.
neXtProt; NX_Q8IYB3; -.
OpenTargets; ENSG00000133226; -.
PharmGKB; PA38177; -.
eggNOG; KOG2146; Eukaryota.
eggNOG; ENOG4111IMU; LUCA.
GeneTree; ENSGT00730000111080; -.
HOGENOM; HOG000231139; -.
HOVERGEN; HBG054044; -.
InParanoid; Q8IYB3; -.
KO; K13171; -.
PhylomeDB; Q8IYB3; -.
TreeFam; TF318972; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
ChiTaRS; SRRM1; human.
EvolutionaryTrace; Q8IYB3; -.
GeneWiki; SRRM1; -.
GenomeRNAi; 10250; -.
PMAP-CutDB; Q8IYB3; -.
PRO; PR:Q8IYB3; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000133226; -.
CleanEx; HS_SRRM1; -.
ExpressionAtlas; Q8IYB3; baseline and differential.
Genevisible; Q8IYB3; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
InterPro; IPR002483; PWI_dom.
InterPro; IPR036483; PWI_dom_sf.
Pfam; PF01480; PWI; 1.
SMART; SM00311; PWI; 1.
SUPFAM; SSF101233; SSF101233; 1.
PROSITE; PS51025; PWI; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Citrullination;
Complete proteome; Direct protein sequencing; DNA-binding;
Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; RNA-binding;
Spliceosome; Ubl conjugation.
CHAIN 1 904 Serine/arginine repetitive matrix protein
1.
/FTId=PRO_0000076326.
DOMAIN 27 126 PWI. {ECO:0000255|PROSITE-
ProRule:PRU00627}.
REGION 1 156 Necessary for mRNA 3'-end cleavage and
cytoplasmic accumulation.
REGION 1 151 Necessary for DNA and RNA-binding.
REGION 300 688 Necessary for speckles and matrix
localization.
COMPBIAS 163 726 Arg-rich.
COMPBIAS 210 417 Pro-rich.
COMPBIAS 278 756 Ser-rich.
COMPBIAS 550 799 Pro-rich.
COMPBIAS 809 835 Lys-rich.
COMPBIAS 836 865 Ala-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
MOD_RES 7 7 Citrulline. {ECO:0000250}.
MOD_RES 140 140 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 220 220 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 227 227 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 241 241 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 260 260 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 389 389 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|Ref.5}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|Ref.5}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 406 406 Phosphothreonine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 416 416 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 429 429 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 436 436 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231}.
MOD_RES 524 524 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 528 528 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 549 549 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 555 555 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 562 562 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 572 572 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 574 574 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 581 581 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 596 596 Phosphotyrosine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 597 597 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 607 607 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 614 614 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 628 628 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 638 638 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000250|UniProtKB:Q52KI8}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 705 705 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 707 707 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 713 713 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 718 718 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 740 740 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 748 748 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 756 756 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 773 773 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 777 777 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 778 778 Phosphothreonine.
{ECO:0000250|UniProtKB:Q52KI8}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 791 791 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 793 793 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 797 797 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 802 802 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 872 872 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 874 874 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 901 901 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 127 127 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 231 231 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 231 231 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 249 249 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 447 447 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 459 459 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 472 472 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 869 869 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 305 308 RSRS -> DKM (in isoform 2).
{ECO:0000303|PubMed:9531537,
ECO:0000303|Ref.2}.
/FTId=VSP_016522.
VAR_SEQ 407 407 Missing (in isoform 2).
{ECO:0000303|PubMed:9531537,
ECO:0000303|Ref.2}.
/FTId=VSP_016523.
VARIANT 170 170 R -> H (in dbSNP:rs17857102).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_024065.
MUTAGEN 20 20 K->A: Strongly reduces DNA and RNA-
binding. {ECO:0000269|PubMed:12600940}.
MUTAGEN 22 22 K->A: Strongly reduces DNA and RNA-
binding. {ECO:0000269|PubMed:12600940}.
MUTAGEN 23 23 K->A: Strongly reduces DNA and RNA-
binding. {ECO:0000269|PubMed:12600940}.
CONFLICT 269 269 K -> Q (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 275 275 R -> Q (in Ref. 4; AAH36187).
{ECO:0000305}.
CONFLICT 413 413 H -> D (in Ref. 1 and 2). {ECO:0000305}.
HELIX 33 36 {ECO:0000244|PDB:1MP1}.
TURN 40 42 {ECO:0000244|PDB:1MP1}.
HELIX 46 48 {ECO:0000244|PDB:1MP1}.
HELIX 49 60 {ECO:0000244|PDB:1MP1}.
HELIX 66 74 {ECO:0000244|PDB:1MP1}.
STRAND 77 79 {ECO:0000244|PDB:1MP1}.
HELIX 82 89 {ECO:0000244|PDB:1MP1}.
TURN 90 92 {ECO:0000244|PDB:1MP1}.
HELIX 96 112 {ECO:0000244|PDB:1MP1}.
STRAND 115 118 {ECO:0000244|PDB:1MP1}.
HELIX 121 124 {ECO:0000244|PDB:1MP1}.
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


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29-447 MATR3 is localized in the nuclear matrix. It may play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network.The protein encoded by this 0.1 mg
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