SRSF7_HUMAN
ID SRSF7_HUMAN Reviewed; 238 AA.
AC Q16629; B4DLU6; G5E9M3; Q564D3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Serine/arginine-rich splicing factor 7;
DE AltName: Full=Splicing factor 9G8;
DE AltName: Full=Splicing factor, arginine/serine-rich 7;
GN Name=SRSF7; Synonyms=SFRS7;
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], AND PROTEIN SEQUENCE OF 7-24; 30-58 AND 79-87.
RC TISSUE=Placenta;
RX PubMed=8013463; DOI=10.1002/j.1460-2075.1994.tb06554.x;
RA Cavaloc Y., Popielarz M., Fuchs J.-P., Gattoni R., Stevenin J.;
RT "Characterization and cloning of the human splicing factor 9G8: a novel 35
RT kDa factor of the serine/arginine protein family.";
RL EMBO J. 13:2639-2649(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Placenta;
RX PubMed=7629084; DOI=10.1074/jbc.270.30.17830;
RA Popielarz M., Cavaloc Y., Mattei M.-G., Gattoni R., Stevenin J.;
RT "The gene encoding human splicing factor 9G8. Structure, chromosomal
RT localization, and expression of alternatively processed transcripts.";
RL J. Biol. Chem. 270:17830-17835(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=20857263; DOI=10.1007/s00795-010-0492-5;
RA Kimura T., Hashimoto I., Nishizawa M., Ito S., Yamada H.;
RT "Novel cis-active structures in the coding region mediate CRM1-dependent
RT nuclear export of IFN-alpha 1 mRNA.";
RL Med. Mol. Morphol. 43:145-157(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Guo J.H., Yu L.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of human aging-associated gene.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, Prostate, and Skin;
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 [11]
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 [12]
RP INTERACTION WITH CCNL1; CDC2L1 AND CDC2L2.
RX PubMed=12501247; DOI=10.1074/jbc.m210057200;
RA Hu D., Mayeda A., Trembley J.H., Lahti J.M., Kidd V.J.;
RT "CDK11 complexes promote pre-mRNA splicing.";
RL J. Biol. Chem. 278:8623-8629(2003).
RN [13]
RP FUNCTION IN MRNA EXPORT, AND 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 [14]
RP INTERACTION WITH CCNL2.
RX PubMed=14684736; DOI=10.1074/jbc.m312895200;
RA Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.;
RT "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in
RT pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma
RT cells.";
RL J. Biol. Chem. 279:11639-11648(2004).
RN [15]
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 [16]
RP FUNCTION.
RX PubMed=15009664; DOI=10.1046/j.1471-4159.2003.02232.x;
RA Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.;
RT "Tau exon 10, whose missplicing causes frontotemporal dementia, is
RT regulated by an intricate interplay of cis elements and trans factors.";
RL J. Neurochem. 88:1078-1090(2004).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-194 AND SER-196, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, 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 [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-194; SER-231 AND
RP SER-233, 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-163; SER-165 AND
RP SER-167, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [26]
RP STRUCTURE BY NMR OF 12-98, RNA-BINDING, INTERACTION WITH NXF1, AND
RP MUTAGENESIS OF 87-ARG-ARG-88 AND 97-ARG-ARG-98.
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).
CC -!- FUNCTION: Required for pre-mRNA splicing. Can also modulate alternative
CC splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May
CC function as export adapter involved in mRNA nuclear export such as of
CC histone H2A. Binds mRNA which is thought to be transferred to the NXF1-
CC NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-
CC binding activity. RNA-binding is semi-sequence specific.
CC {ECO:0000269|PubMed:11336712, ECO:0000269|PubMed:12667464,
CC ECO:0000269|PubMed:15009664, ECO:0000269|PubMed:18364396}.
CC -!- SUBUNIT: Found in large molecular weight complexes containing CCNL1 and
CC the p110 isoforms of either CDC2L1 or CDC2L2 (PubMed:12501247,
CC PubMed:14684736). Interacts with CCNL2 and CPSF6 (PubMed:15169763,
CC PubMed:12501247). Interacts with NXF1 (PubMed:12667464,
CC PubMed:17036044). Interacts with YTHDC1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BL97, ECO:0000269|PubMed:12501247,
CC ECO:0000269|PubMed:12667464, ECO:0000269|PubMed:14684736,
CC ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:17036044}.
CC -!- INTERACTION:
CC Q16629; P49759-3: CLK1; NbExp=3; IntAct=EBI-398885, EBI-11981867;
CC Q16629; Q9NQ29-3: LUC7L; NbExp=3; IntAct=EBI-398885, EBI-6654742;
CC Q16629; Q9Y383: LUC7L2; NbExp=7; IntAct=EBI-398885, EBI-352851;
CC Q16629; Q9UBU9: NXF1; NbExp=4; IntAct=EBI-398885, EBI-398874;
CC Q16629; Q8NAV1: PRPF38A; NbExp=3; IntAct=EBI-398885, EBI-715374;
CC Q16629; Q7Z6E9: RBBP6; NbExp=3; IntAct=EBI-398885, EBI-2117026;
CC Q16629; Q15287: RNPS1; NbExp=3; IntAct=EBI-398885, EBI-395959;
CC Q16629; O00560: SDCBP; NbExp=6; IntAct=EBI-398885, EBI-727004;
CC Q16629; Q96SB4: SRPK1; NbExp=2; IntAct=EBI-398885, EBI-539478;
CC Q16629; P78362: SRPK2; NbExp=2; IntAct=EBI-398885, EBI-593303;
CC Q16629; Q9JKL7: Srek1; Xeno; NbExp=3; IntAct=EBI-398885, EBI-6452221;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11336712}. Cytoplasm
CC {ECO:0000269|PubMed:11336712}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Isoforms, often lacking the RS domain and differentially
CC expressed in fetal tissues, may be involved in modulation of 9G8
CC function.;
CC Name=1;
CC IsoId=Q16629-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16629-2; Sequence=VSP_005872, VSP_005873;
CC Name=3;
CC IsoId=Q16629-3; Sequence=VSP_005874, VSP_005875;
CC Name=4;
CC IsoId=Q16629-4; Sequence=VSP_045840;
CC -!- TISSUE SPECIFICITY: Brain, liver, kidney and lung.
CC -!- PTM: Extensively phosphorylated on serine residues in the RS domain.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; L22253; AAA35495.1; -; mRNA.
DR EMBL; L41887; AAA88098.1; -; Genomic_DNA.
DR EMBL; AB445102; BAI99737.1; -; mRNA.
DR EMBL; AY166860; AAN87842.1; -; mRNA.
DR EMBL; BT006745; AAP35391.1; -; mRNA.
DR EMBL; AY513287; AAT08040.1; -; mRNA.
DR EMBL; AK297161; BAG59658.1; -; mRNA.
DR EMBL; AC074366; AAX93102.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00365.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00366.1; -; Genomic_DNA.
DR EMBL; BC000997; AAH00997.1; -; mRNA.
DR EMBL; BC017369; AAH17369.1; -; mRNA.
DR EMBL; BC017908; AAH17908.1; -; mRNA.
DR EMBL; BC022328; AAH22328.1; -; mRNA.
DR CCDS; CCDS33183.1; -. [Q16629-1]
DR CCDS; CCDS56115.1; -. [Q16629-4]
DR PIR; A57198; A57198.
DR RefSeq; NP_001026854.1; NM_001031684.2. [Q16629-1]
DR RefSeq; NP_001182375.1; NM_001195446.1. [Q16629-4]
DR PDB; 2HVZ; NMR; -; A=12-98.
DR PDBsum; 2HVZ; -.
DR AlphaFoldDB; Q16629; -.
DR BMRB; Q16629; -.
DR SMR; Q16629; -.
DR BioGRID; 112330; 359.
DR CORUM; Q16629; -.
DR DIP; DIP-31790N; -.
DR IntAct; Q16629; 75.
DR MINT; Q16629; -.
DR STRING; 9606.ENSP00000325905; -.
DR GlyGen; Q16629; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16629; -.
DR MetOSite; Q16629; -.
DR PhosphoSitePlus; Q16629; -.
DR SwissPalm; Q16629; -.
DR BioMuta; SRSF7; -.
DR DMDM; 3929380; -.
DR SWISS-2DPAGE; P99058; -.
DR EPD; Q16629; -.
DR jPOST; Q16629; -.
DR MassIVE; Q16629; -.
DR MaxQB; Q16629; -.
DR PaxDb; Q16629; -.
DR PeptideAtlas; Q16629; -.
DR PRIDE; Q16629; -.
DR ProteomicsDB; 33982; -.
DR ProteomicsDB; 60976; -. [Q16629-1]
DR ProteomicsDB; 60977; -. [Q16629-2]
DR ProteomicsDB; 60978; -. [Q16629-3]
DR TopDownProteomics; Q16629-1; -. [Q16629-1]
DR TopDownProteomics; Q16629-2; -. [Q16629-2]
DR TopDownProteomics; Q16629-3; -. [Q16629-3]
DR TopDownProteomics; Q16629-4; -. [Q16629-4]
DR Antibodypedia; 29517; 268 antibodies from 32 providers.
DR DNASU; 6432; -.
DR Ensembl; ENST00000313117.11; ENSP00000325905.6; ENSG00000115875.19. [Q16629-1]
DR Ensembl; ENST00000431066.5; ENSP00000398159.1; ENSG00000115875.19. [Q16629-3]
DR Ensembl; ENST00000443213.5; ENSP00000402544.1; ENSG00000115875.19. [Q16629-3]
DR Ensembl; ENST00000446327.6; ENSP00000402264.2; ENSG00000115875.19. [Q16629-4]
DR GeneID; 6432; -.
DR KEGG; hsa:6432; -.
DR MANE-Select; ENST00000313117.11; ENSP00000325905.6; NM_001031684.3; NP_001026854.1.
DR UCSC; uc002rqz.3; human. [Q16629-1]
DR CTD; 6432; -.
DR DisGeNET; 6432; -.
DR GeneCards; SRSF7; -.
DR HGNC; HGNC:10789; SRSF7.
DR HPA; ENSG00000115875; Low tissue specificity.
DR MIM; 600572; gene.
DR neXtProt; NX_Q16629; -.
DR OpenTargets; ENSG00000115875; -.
DR PharmGKB; PA35705; -.
DR VEuPathDB; HostDB:ENSG00000115875; -.
DR eggNOG; KOG0107; Eukaryota.
DR GeneTree; ENSGT00910000144115; -.
DR InParanoid; Q16629; -.
DR OMA; VERSHGM; -.
DR OrthoDB; 1533297at2759; -.
DR PhylomeDB; Q16629; -.
DR TreeFam; TF351858; -.
DR PathwayCommons; Q16629; -.
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-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q16629; -.
DR SIGNOR; Q16629; -.
DR BioGRID-ORCS; 6432; 807 hits in 1082 CRISPR screens.
DR ChiTaRS; SRSF7; human.
DR EvolutionaryTrace; Q16629; -.
DR GeneWiki; SFRS7; -.
DR GenomeRNAi; 6432; -.
DR Pharos; Q16629; Tbio.
DR PRO; PR:Q16629; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q16629; protein.
DR Bgee; ENSG00000115875; Expressed in ganglionic eminence and 211 other tissues.
DR ExpressionAtlas; Q16629; baseline and differential.
DR Genevisible; Q16629; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IDA:ProtInc.
DR CDD; cd12646; RRM_SRSF7; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR IDEAL; IID00214; -.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034651; SRSF7_RRM.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57756; SSF57756; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; Transport; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..238
FT /note="Serine/arginine-rich splicing factor 7"
FT /id="PRO_0000081932"
FT DOMAIN 11..84
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REPEAT 153..160
FT /note="1"
FT REPEAT 161..168
FT /note="2"
FT REPEAT 169..176
FT /note="3"
FT REPEAT 177..184
FT /note="4"
FT REPEAT 211..218
FT /note="5; approximate"
FT REPEAT 219..226
FT /note="6; approximate"
FT ZN_FING 104..120
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 81..98
FT /note="Sufficient for interaction with NXF1"
FT REGION 123..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..226
FT /note="6 X 8 AA repeats of R-R-S-R-S-X-S-X"
FT COMPBIAS 123..176
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..217
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL97"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BL97"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 130..135
FT /note="SRSRSH -> AENLRR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005872"
FT VAR_SEQ 130..132
FT /note="SRS -> YLF (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005874"
FT VAR_SEQ 133..238
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005875"
FT VAR_SEQ 136..238
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005873"
FT VAR_SEQ 209..220
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045840"
FT MUTAGEN 87..88
FT /note="RR->EE: Abolishes interaction with NXF1."
FT /evidence="ECO:0000269|PubMed:17036044"
FT MUTAGEN 97..98
FT /note="RR->EE: Abolishes interaction with NXF1."
FT /evidence="ECO:0000269|PubMed:17036044"
FT CONFLICT 56
FT /note="D -> G (in Ref. 7; BAG59658)"
FT /evidence="ECO:0000305"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:2HVZ"
FT HELIX 24..34
FT /evidence="ECO:0007829|PDB:2HVZ"
FT STRAND 38..53
FT /evidence="ECO:0007829|PDB:2HVZ"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:2HVZ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2HVZ"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:2HVZ"
SQ SEQUENCE 238 AA; 27367 MW; 49136754D9630853 CRC64;
MSRYGRYGGE TKVYVGNLGT GAGKGELERA FSYYGPLRTV WIARNPPGFA FVEFEDPRDA
EDAVRGLDGK VICGSRVRVE LSTGMPRRSR FDRPPARRPF DPNDRCYECG EKGHYAYDCH
RYSRRRRSRS RSRSHSRSRG RRYSRSRSRS RGRRSRSASP RRSRSISLRR SRSASLRRSR
SGSIKGSRYF QSPSRSRSRS RSISRPRSSR SKSRSPSPKR SRSPSGSPRR SASPERMD
