SRSF3_HUMAN
ID SRSF3_HUMAN Reviewed; 164 AA.
AC P84103; B4E241; O08831; P23152; Q5R3K0;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/arginine-rich splicing factor 3;
DE AltName: Full=Pre-mRNA-splicing factor SRP20;
DE AltName: Full=Splicing factor, arginine/serine-rich 3;
GN Name=SRSF3; Synonyms=SFRS3, SRP20;
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 1), AND PROTEIN SEQUENCE OF 29-37 AND
RP 54-64.
RX PubMed=1577277; DOI=10.1101/gad.6.5.837;
RA Zahler A.M., Lane W.S., Stolk J.A., Roth M.B.;
RT "SR proteins: a conserved family of pre-mRNA splicing factors.";
RL Genes Dev. 6:837-847(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu W.L., Wang M., Tang D., Rodgers G.;
RT "Identification and characterization of novel full-length cDNAs
RT differentially expressed in hematopoietic lineages.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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 [8]
RP INTERACTION WITH SREK1.
RX PubMed=10757789; DOI=10.1128/mcb.20.9.3049-3057.2000;
RA Barnard D.C., Patton J.G.;
RT "Identification and characterization of a novel serine-arginine-rich
RT splicing regulatory protein.";
RL Mol. Cell. Biol. 20:3049-3057(2000).
RN [9]
RP FUNCTION IN MRNA EXPORT, AND SUBCELLULAR LOCATION.
RX PubMed=11336712; DOI=10.1016/s1097-2765(01)00233-7;
RA Huang Y., Steitz J.A.;
RT "Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of
RT mRNA.";
RL Mol. Cell 7:899-905(2001).
RN [10]
RP INTERACTION WITH NXF1.
RX PubMed=12667464; DOI=10.1016/s1097-2765(03)00089-3;
RA Huang Y., Gattoni R., Stevenin J., Steitz J.A.;
RT "SR splicing factors serve as adapter proteins for TAP-dependent mRNA
RT export.";
RL Mol. Cell 11:837-843(2003).
RN [11]
RP INTERACTION WITH RBMY1A1.
RX PubMed=15595951; DOI=10.1111/j.1365-2605.2004.00496.x;
RA Elliott D.J.;
RT "The role of potential splicing factors including RBMY, RBMX, hnRNPG-T and
RT STAR proteins in spermatogenesis.";
RL Int. J. Androl. 27:328-334(2004).
RN [12]
RP INTERACTION WITH CPSF6.
RX PubMed=15169763; DOI=10.1074/jbc.m403927200;
RA Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.;
RT "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im
RT mediate RNA binding, protein-protein interactions, and subcellular
RT localization.";
RL J. Biol. Chem. 279:35788-35797(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP FUNCTION IN MRNA EXPORT.
RX PubMed=18364396; DOI=10.1073/pnas.0709167105;
RA Hautbergue G.M., Hung M.L., Golovanov A.P., Lian L.Y., Wilson S.A.;
RT "Mutually exclusive interactions drive handover of mRNA from export
RT adaptors to TAP.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5154-5159(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23, 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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP STRUCTURE BY NMR OF 1-86, RNA-BINDING, FUNCTION, INTERACTION WITH NXF1, AND
RP MUTAGENESIS OF ARG-86; ARG-88 AND ARG-90.
RX PubMed=17036044; DOI=10.1038/sj.emboj.7601385;
RA Hargous Y., Hautbergue G.M., Tintaru A.M., Skrisovska L., Golovanov A.P.,
RA Stevenin J., Lian L.Y., Wilson S.A., Allain F.H.;
RT "Molecular basis of RNA recognition and TAP binding by the SR proteins
RT SRp20 and 9G8.";
RL EMBO J. 25:5126-5137(2006).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH YTHDC1.
RX PubMed=26876937; DOI=10.1016/j.molcel.2016.01.012;
RA Xiao W., Adhikari S., Dahal U., Chen Y.S., Hao Y.J., Sun B.F., Sun H.Y.,
RA Li A., Ping X.L., Lai W.Y., Wang X., Ma H.L., Huang C.M., Yang Y.,
RA Huang N., Jiang G.B., Wang H.L., Zhou Q., Wang X.J., Zhao Y.L., Yang Y.G.;
RT "Nuclear m(6)A reader YTHDC1 regulates mRNA splicing.";
RL Mol. Cell 61:507-519(2016).
RN [22]
RP FUNCTION, AND INTERACTION WITH YTHDC1.
RX PubMed=28984244; DOI=10.7554/elife.31311;
RA Roundtree I.A., Luo G.Z., Zhang Z., Wang X., Zhou T., Cui Y., Sha J.,
RA Huang X., Guerrero L., Xie P., He E., Shen B., He C.;
RT "YTHDC1 mediates nuclear export of N6-methyladenosine methylated mRNAs.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Splicing factor that specifically promotes exon-inclusion
CC during alternative splicing (PubMed:26876937). Interaction with YTHDC1,
CC a RNA-binding protein that recognizes and binds N6-methyladenosine
CC (m6A)-containing RNAs, promotes recruitment of SRSF3 to its mRNA-
CC binding elements adjacent to m6A sites, leading to exon-inclusion
CC during alternative splicing (PubMed:26876937). Also functions as export
CC adapter involved in mRNA nuclear export (PubMed:11336712,
CC PubMed:18364396, PubMed:28984244). Binds mRNA which is thought to be
CC transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway);
CC enhances NXF1-NXT1 RNA-binding activity (PubMed:11336712,
CC PubMed:18364396). Involved in nuclear export of m6A-containing mRNAs
CC via interaction with YTHDC1: interaction with YTHDC1 facilitates m6A-
CC containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear
CC export (PubMed:28984244). RNA-binding is semi-sequence specific
CC (PubMed:17036044). {ECO:0000269|PubMed:11336712,
CC ECO:0000269|PubMed:17036044, ECO:0000269|PubMed:18364396,
CC ECO:0000269|PubMed:26876937, ECO:0000269|PubMed:28984244}.
CC -!- SUBUNIT: Interacts with CPSF6 (PubMed:15169763). Interacts with RBMY1A1
CC (PubMed:15595951). Interacts with SREK1/SFRS12 (PubMed:10757789).
CC Interacts with NXF1 (PubMed:12667464, PubMed:17036044). Interacts with
CC YTHDC1, leading to recruitment to RNA elements adjacent to m6A sites
CC (PubMed:26876937, PubMed:28984244). {ECO:0000269|PubMed:10757789,
CC ECO:0000269|PubMed:12667464, ECO:0000269|PubMed:15169763,
CC ECO:0000269|PubMed:15595951, ECO:0000269|PubMed:17036044,
CC ECO:0000269|PubMed:26876937, ECO:0000269|PubMed:28984244}.
CC -!- INTERACTION:
CC P84103; Q14011: CIRBP; NbExp=3; IntAct=EBI-372557, EBI-538850;
CC P84103; P49759-3: CLK1; NbExp=3; IntAct=EBI-372557, EBI-11981867;
CC P84103; P49760: CLK2; NbExp=3; IntAct=EBI-372557, EBI-750020;
CC P84103; P49761: CLK3; NbExp=3; IntAct=EBI-372557, EBI-745579;
CC P84103; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-372557, EBI-741032;
CC P84103; P09429: HMGB1; NbExp=3; IntAct=EBI-372557, EBI-389432;
CC P84103; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-372557, EBI-7060731;
CC P84103; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-372557, EBI-739832;
CC P84103; Q9UBU9: NXF1; NbExp=4; IntAct=EBI-372557, EBI-398874;
CC P84103; Q15366: PCBP2; NbExp=3; IntAct=EBI-372557, EBI-945799;
CC P84103; P57721-2: PCBP3; NbExp=3; IntAct=EBI-372557, EBI-11983983;
CC P84103; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-372557, EBI-10329013;
CC P84103; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-372557, EBI-1567797;
CC P84103; P98179: RBM3; NbExp=3; IntAct=EBI-372557, EBI-2949699;
CC P84103; P38159: RBMX; NbExp=3; IntAct=EBI-372557, EBI-743526;
CC P84103; Q15287: RNPS1; NbExp=3; IntAct=EBI-372557, EBI-395959;
CC P84103; P32969: RPL9P9; NbExp=3; IntAct=EBI-372557, EBI-358122;
CC P84103; O00560: SDCBP; NbExp=3; IntAct=EBI-372557, EBI-727004;
CC P84103; Q9BRL6-2: SRSF8; NbExp=3; IntAct=EBI-372557, EBI-10976394;
CC P84103; Q01081: U2AF1; NbExp=4; IntAct=EBI-372557, EBI-632461;
CC P84103; P26368-2: U2AF2; NbExp=3; IntAct=EBI-372557, EBI-11097439;
CC P84103; Q9JKL7: Srek1; Xeno; NbExp=3; IntAct=EBI-372557, EBI-6452221;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11336712}. Nucleus
CC speckle {ECO:0000269|PubMed:26876937}. Cytoplasm
CC {ECO:0000269|PubMed:11336712}. Note=Recruited to nuclear speckles
CC following interaction with YTHDC1. {ECO:0000269|PubMed:26876937}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P84103-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P84103-2; Sequence=VSP_056243;
CC -!- PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Extensively
CC phosphorylated on serine residues in the RS domain.
CC {ECO:0000250|UniProtKB:P84104}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SRSF3ID42279ch6p21.html";
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DR EMBL; L10838; AAA36648.1; -; mRNA.
DR EMBL; AF107405; AAD44523.1; -; mRNA.
DR EMBL; AK304097; BAG65003.1; -; mRNA.
DR EMBL; BT007017; AAP35663.1; -; mRNA.
DR EMBL; Z85986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03898.1; -; Genomic_DNA.
DR EMBL; BC000914; AAH00914.1; -; mRNA.
DR EMBL; BC069018; AAH69018.1; -; mRNA.
DR CCDS; CCDS4823.1; -. [P84103-1]
DR PIR; I54089; I54089.
DR RefSeq; NP_003008.1; NM_003017.4. [P84103-1]
DR PDB; 2I2Y; NMR; -; A=1-86.
DR PDB; 2I38; NMR; -; A=1-86.
DR PDBsum; 2I2Y; -.
DR PDBsum; 2I38; -.
DR AlphaFoldDB; P84103; -.
DR SMR; P84103; -.
DR BioGRID; 112326; 435.
DR CORUM; P84103; -.
DR DIP; DIP-32961N; -.
DR IntAct; P84103; 92.
DR MINT; P84103; -.
DR STRING; 9606.ENSP00000362820; -.
DR GlyGen; P84103; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P84103; -.
DR PhosphoSitePlus; P84103; -.
DR SwissPalm; P84103; -.
DR BioMuta; SRSF3; -.
DR DMDM; 51338672; -.
DR EPD; P84103; -.
DR jPOST; P84103; -.
DR MassIVE; P84103; -.
DR MaxQB; P84103; -.
DR PaxDb; P84103; -.
DR PeptideAtlas; P84103; -.
DR PRIDE; P84103; -.
DR ProteomicsDB; 57753; -. [P84103-1]
DR ProteomicsDB; 5800; -.
DR TopDownProteomics; P84103-1; -. [P84103-1]
DR Antibodypedia; 29693; 286 antibodies from 31 providers.
DR DNASU; 6428; -.
DR Ensembl; ENST00000373715.11; ENSP00000362820.5; ENSG00000112081.17. [P84103-1]
DR Ensembl; ENST00000477442.6; ENSP00000436036.1; ENSG00000112081.17. [P84103-2]
DR Ensembl; ENST00000620941.1; ENSP00000482833.1; ENSG00000112081.17. [P84103-1]
DR GeneID; 6428; -.
DR KEGG; hsa:6428; -.
DR MANE-Select; ENST00000373715.11; ENSP00000362820.5; NM_003017.5; NP_003008.1.
DR UCSC; uc003omj.4; human. [P84103-1]
DR CTD; 6428; -.
DR DisGeNET; 6428; -.
DR GeneCards; SRSF3; -.
DR HGNC; HGNC:10785; SRSF3.
DR HPA; ENSG00000112081; Low tissue specificity.
DR MIM; 603364; gene.
DR neXtProt; NX_P84103; -.
DR OpenTargets; ENSG00000112081; -.
DR PharmGKB; PA35701; -.
DR VEuPathDB; HostDB:ENSG00000112081; -.
DR eggNOG; KOG0107; Eukaryota.
DR GeneTree; ENSGT00910000144115; -.
DR HOGENOM; CLU_012062_20_2_1; -.
DR InParanoid; P84103; -.
DR OMA; EMHRDSC; -.
DR PhylomeDB; P84103; -.
DR TreeFam; TF351858; -.
DR PathwayCommons; P84103; -.
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; P84103; -.
DR SIGNOR; P84103; -.
DR BioGRID-ORCS; 6428; 808 hits in 1082 CRISPR screens.
DR ChiTaRS; SRSF3; human.
DR EvolutionaryTrace; P84103; -.
DR GeneWiki; SFRS3; -.
DR GenomeRNAi; 6428; -.
DR Pharos; P84103; Tbio.
DR PRO; PR:P84103; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P84103; protein.
DR Bgee; ENSG00000112081; Expressed in ventricular zone and 208 other tissues.
DR ExpressionAtlas; P84103; baseline and differential.
DR Genevisible; P84103; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
DR GO; GO:0070878; F:primary miRNA binding; IMP:ARUK-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0031053; P:primary miRNA processing; IMP:ARUK-UCL.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00204; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; mRNA processing; mRNA splicing; mRNA transport;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transport.
FT CHAIN 1..164
FT /note="Serine/arginine-rich splicing factor 3"
FT /id="PRO_0000081923"
FT DOMAIN 10..83
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 119..133
FT /note="B-1"
FT REPEAT 149..164
FT /note="B-2"
FT REGION 1..90
FT /note="Sufficient for interaction with NXF1"
FT REGION 81..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..164
FT /note="2 X approximate repeats, basic"
FT COMPBIAS 95..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 115..164
FT /note="SPRRRSFSRSRSRSLSRDRRRERSLSRERNHKPSRSFSRSRSRSRSNERK
FT -> VTIMSLLTTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056243"
FT MUTAGEN 86
FT /note="R->E: Abolishes interaction with NXF1."
FT /evidence="ECO:0000269|PubMed:17036044"
FT MUTAGEN 88
FT /note="R->E: Abolishes interaction with NXF1."
FT /evidence="ECO:0000269|PubMed:17036044"
FT MUTAGEN 90
FT /note="R->E: Abolishes interaction with NXF1."
FT /evidence="ECO:0000269|PubMed:17036044"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:2I2Y"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2I38"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:2I2Y"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2I2Y"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2I2Y"
SQ SEQUENCE 164 AA; 19330 MW; 02F0A5EE33FF28A0 CRC64;
MHRDSCPLDC KVYVGNLGNN GNKTELERAF GYYGPLRSVW VARNPPGFAF VEFEDPRDAA
DAVRELDGRT LCGCRVRVEL SNGEKRSRNR GPPPSWGRRP RDDYRRRSPP PRRRSPRRRS
FSRSRSRSLS RDRRRERSLS RERNHKPSRS FSRSRSRSRS NERK
