ID RUXF_HUMAN Reviewed; 86 AA. AC P62306; A2VCR2; B2R498; Q15356; Q6IBQ1; Q6P4I0; DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 29-MAY-2024, entry version 177. DE RecName: Full=Small nuclear ribonucleoprotein F; DE Short=snRNP-F; DE AltName: Full=Sm protein F; DE Short=Sm-F; DE Short=SmF; GN Name=SNRPF; Synonyms=PBSCF; 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]. RC TISSUE=Cervix carcinoma; RX PubMed=7744013; DOI=10.1002/j.1460-2075.1995.tb07199.x; RA Hermann H., Fabrizio P., Raker V.A., Foulaki K., Hornig H., Brahms H., RA Luehrmann R.; RT "snRNP Sm proteins share two evolutionarily conserved sequence motifs which RT are involved in Sm protein-protein interactions."; RL EMBO J. 14:2076-2088(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; 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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon; 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 [6] RP PROTEIN SEQUENCE OF 2-22 AND 66-86, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP IDENTIFICATION IN THE U7 SNRNP COMPLEX, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11574479; DOI=10.1093/emboj/20.19.5470; RA Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.; RT "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new RT 14 kDa Sm D1-like protein."; RL EMBO J. 20:5470-5479(2001). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. 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 [9] RP FUNCTION OF THE U7 SNRNP COMPLEX. RX PubMed=12975319; DOI=10.1101/gad.274403; RA Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U., RA Schuemperli D.; RT "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN RT complex and the role of a new component, Lsm11, in histone RNA RT processing."; RL Genes Dev. 17:2321-2333(2003). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [11] RP IDENTIFICATION IN A COMPLEX WITH THE MINOR SPLICEOSOME, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=15146077; DOI=10.1261/rna.7320604; RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., RA Tuschl T., Luehrmann R.; RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in RT the U2-dependent spliceosome."; RL RNA 10:929-941(2004). RN [12] RP IDENTIFICATION IN THE SMN-SM COMPLEX. RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005; RA Golembe T.J., Yong J., Dreyfuss G.; RT "Specific sequence features, recognized by the SMN complex, identify snRNAs RT and determine their fate as snRNPs."; RL Mol. Cell. Biol. 25:10989-11004(2005). RN [13] RP FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, RP IDENTIFICATION IN SMN-SM COMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020; RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., RA Englbrecht C., Sickmann A., Stark H., Fischer U.; RT "An assembly chaperone collaborates with the SMN complex to generate RT spliceosomal SnRNPs."; RL Cell 135:497-509(2008). RN [14] 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 [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP, FUNCTION, RP AND SUBUNIT. RX PubMed=19325628; DOI=10.1038/nature07851; RA Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.; RT "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."; RL Nature 458:475-480(2009). RN [17] {ECO:0007744|PDB:5XJL} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SNRPD1; SNRPD2; RP SNRPE; SNRPG; SMN1 AND GEMIN2, AND INTERACTION WITH GEMIN2; SNRPE AND RP SNRPD2. RX PubMed=21816274; DOI=10.1016/j.cell.2011.06.043; RA Zhang R., So B.R., Li P., Yong J., Glisovic T., Wan L., Dreyfuss G.; RT "Structure of a key intermediate of the SMN complex reveals Gemin2's RT crucial function in snRNP assembly."; RL Cell 146:384-395(2011). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP, AND RP SUBUNIT. RX PubMed=21516107; DOI=10.1038/nature09956; RA Leung A.K., Nagai K., Li J.; RT "Structure of the spliceosomal U4 snRNP core domain and its implication for RT snRNP biogenesis."; RL Nature 473:536-539(2011). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN 6S PICLN-SM COMPLEX, RP IDENTIFICATION IN 6S PICLN-SM COMPLEX, AND FUNCTION IN CORE U1 SNRNP RP BIOGENESIS. RX PubMed=23333303; DOI=10.1016/j.molcel.2012.12.009; RA Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K., RA Stark H., Schindelin H., Fischer U.; RT "Structural basis of assembly chaperone-mediated snRNP formation."; RL Mol. Cell 49:692-703(2013). RN [20] {ECO:0007744|PDB:4PJO} RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-75, AND SUBUNIT. RX PubMed=25555158; DOI=10.7554/elife.04986; RA Kondo Y., Oubridge C., van Roon A.M., Nagai K.; RT "Crystal structure of human U1 snRNP, a small nuclear ribonucleoprotein RT particle, reveals the mechanism of 5' splice site recognition."; RL Elife 4:0-0(2015). RN [21] {ECO:0007744|PDB:3JCR} RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR LOCATION, RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=26912367; DOI=10.1126/science.aad2085; RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H., RA Luhrmann R., Stark H.; RT "Molecular architecture of the human U4/U6.U5 tri-snRNP."; RL Science 351:1416-1420(2016). RN [22] {ECO:0007744|PDB:5XJC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033; RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.; RT "An Atomic Structure of the Human Spliceosome."; RL Cell 169:918-929(2017). RN [23] {ECO:0007744|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011; RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N., RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for RT Activation."; RL Cell 170:701-713(2017). RN [24] {ECO:0007744|PDB:5MQF} RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=28076346; DOI=10.1038/nature21079; RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K., RA Urlaub H., Kastner B., Stark H., Luhrmann R.; RT "Cryo-EM structure of a human spliceosome activated for step 2 of RT splicing."; RL Nature 542:318-323(2017). RN [25] {ECO:0007744|PDB:5XJQ, ECO:0007744|PDB:5XJR, ECO:0007744|PDB:5XJS} RP X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) IN COMPLEX WITH GEMIN2; SNRPD1; RP SNRPD2; SNRPE; SNRPG AND SMN1, AND INTERACTION WITH GEMIN2; SNRPD2 AND RP SNRPE. RX PubMed=31799625; DOI=10.1093/nar/gkz1135; RA Yi H., Mu L., Shen C., Kong X., Wang Y., Hou Y., Zhang R.; RT "Negative cooperativity between Gemin2 and RNA provides insights into RNA RT selection and the SMN complex's release in snRNP assembly."; RL Nucleic Acids Res. 48:895-911(2020). RN [26] {ECO:0007744|PDB:6Y5Q} RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) IN COMPLEX WITH THE 17S RP U2 SNRNP COMPLEX, FUNCTION, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=32494006; DOI=10.1038/s41586-020-2344-3; RA Zhang Z., Will C.L., Bertram K., Dybkov O., Hartmuth K., Agafonov D.E., RA Hofele R., Urlaub H., Kastner B., Luehrmann R., Stark H.; RT "Molecular architecture of the human 17S U2 snRNP."; RL Nature 583:310-313(2020). RN [27] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). RN [28] {ECO:0007744|PDB:8HK1} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS) IN COMPLEX WITH THE 17S RP U2 SNRNP COMPLEX, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=36797247; DOI=10.1038/s41467-023-36489-x; RA Yang F., Bian T., Zhan X., Chen Z., Xing Z., Larsen N.A., Zhang X., Shi Y.; RT "Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP RT assembly."; RL Nat. Commun. 14:897-897(2023). CC -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the CC spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins CC (snRNPs), the building blocks of the spliceosome (PubMed:11991638, CC PubMed:18984161, PubMed:19325628, PubMed:23333303, PubMed:25555158, CC PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166, CC PubMed:32494006). Component of both the pre-catalytic spliceosome B CC complex and activated spliceosome C complexes (PubMed:11991638, CC PubMed:28076346, PubMed:28502770, PubMed:28781166). As a component of CC the minor spliceosome, involved in the splicing of U12-type introns in CC pre-mRNAs (PubMed:15146077). As part of the U7 snRNP it is involved in CC histone 3'-end processing (PubMed:12975319). CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12975319, CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:23333303, CC ECO:0000269|PubMed:25555158, ECO:0000269|PubMed:26912367, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:32494006}. CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 small CC nuclear ribonucleoproteins (snRNPs), the building blocks of the CC spliceosome (PubMed:11991638, PubMed:19325628, PubMed:21516107, CC PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, CC PubMed:28781166, PubMed:32494006, PubMed:36797247). Most spliceosomal CC snRNPs contain a common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, CC SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein CC ring on the Sm site of the small nuclear RNA to form the core snRNP CC (PubMed:19325628, PubMed:21516107, PubMed:25555158, PubMed:26912367, CC PubMed:28076346, PubMed:28502770, PubMed:28781166). Component of the U1 CC snRNP (PubMed:19325628, PubMed:25555158). The U1 snRNP is composed of CC the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, CC SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins CC SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C (PubMed:19325628, CC PubMed:25555158). Component of the U4/U6-U5 tri-snRNP complex composed CC of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, CC PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3, CC SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and CC USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 CC (PubMed:26912367). Component of the U7 snRNP complex, or U7 Sm protein CC core complex, that is composed of the U7 snRNA and at least LSM10, CC LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not CC contain SNRPD1 and SNRPD2 (PubMed:11574479). Component of the minor CC spliceosome, which splices U12-type introns (PubMed:15146077, CC PubMed:33509932). Part of the SMN-Sm complex that contains SMN1, CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, CC SNRPF and SNRPG; catalyzes core snRNPs assembly (PubMed:16314521, CC PubMed:18984161). Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, CC SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CC CLNS1A/pICln mimics additional Sm proteins and which is unable to CC assemble into the core snRNP (PubMed:18984161, PubMed:23333303). CC Interacts with GEMIN2 (via N-terminus); the interaction is direct CC (PubMed:21816274, PubMed:31799625). Interacts with SNRPD2; the CC interaction is direct (PubMed:21816274, PubMed:31799625). Interacts CC with SNRPE; the interaction is direct (PubMed:21816274, CC PubMed:31799625). {ECO:0000269|PubMed:11574479, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15146077, CC ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:21516107, CC ECO:0000269|PubMed:21816274, ECO:0000269|PubMed:23333303, CC ECO:0000269|PubMed:25555158, ECO:0000269|PubMed:26912367, CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:31799625, CC ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:33509932, CC ECO:0000269|PubMed:36797247}. CC -!- INTERACTION: CC P62306; P54105: CLNS1A; NbExp=5; IntAct=EBI-356900, EBI-724693; CC P62306; P38432: COIL; NbExp=6; IntAct=EBI-356900, EBI-945751; CC P62306; O14893: GEMIN2; NbExp=11; IntAct=EBI-356900, EBI-443648; CC P62306; Q8WXD5: GEMIN6; NbExp=2; IntAct=EBI-356900, EBI-752301; CC P62306; Q9NSC5: HOMER3; NbExp=9; IntAct=EBI-356900, EBI-748420; CC P62306; P42858: HTT; NbExp=3; IntAct=EBI-356900, EBI-466029; CC P62306; Q13422: IKZF1; NbExp=3; IntAct=EBI-356900, EBI-745305; CC P62306; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-356900, EBI-11522367; CC P62306; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-356900, EBI-739832; CC P62306; P62310: LSM3; NbExp=3; IntAct=EBI-356900, EBI-348239; CC P62306; Q9Y4Y9: LSM5; NbExp=11; IntAct=EBI-356900, EBI-373007; CC P62306; Q9UK45: LSM7; NbExp=6; IntAct=EBI-356900, EBI-348372; CC P62306; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-356900, EBI-16439278; CC P62306; Q9H1P3: OSBPL2; NbExp=3; IntAct=EBI-356900, EBI-2828285; CC P62306; P32969: RPL9P9; NbExp=3; IntAct=EBI-356900, EBI-358122; CC P62306; Q15428: SF3A2; NbExp=2; IntAct=EBI-356900, EBI-2462271; CC P62306; P62316: SNRPD2; NbExp=11; IntAct=EBI-356900, EBI-297993; CC P62306; P62304: SNRPE; NbExp=11; IntAct=EBI-356900, EBI-348082; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. CC Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN- CC mediated assembly into core snRNPs occurs in the cytosol before SMN- CC mediated transport to the nucleus to be included in spliceosomes. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X85372; CAA59688.1; -; mRNA. DR EMBL; CR456751; CAG33032.1; -; mRNA. DR EMBL; AK311752; BAG34695.1; -; mRNA. DR EMBL; CH471054; EAW97548.1; -; Genomic_DNA. DR EMBL; BC002505; AAH02505.3; -; mRNA. DR EMBL; BC063397; AAH63397.2; -; mRNA. DR EMBL; BC128452; AAI28453.1; -; mRNA. DR EMBL; BC128453; AAI28454.1; -; mRNA. DR CCDS; CCDS9055.1; -. DR PIR; S55053; S55053. DR RefSeq; NP_003086.1; NM_003095.2. DR PDB; 3CW1; X-ray; 5.49 A; 1/2/F/Z=1-86. DR PDB; 3JCR; EM; 7.00 A; T/t=1-86. DR PDB; 3PGW; X-ray; 4.40 A; F/I=1-86. DR PDB; 4F7U; X-ray; 1.90 A; F/I=1-86. DR PDB; 4PJO; X-ray; 3.30 A; F/T/f/t=1-75. DR PDB; 4V98; X-ray; 3.10 A; AD/AL/AT/Ab/Aj/Ar/Az/BD/BL/BT/Bb/Bj/Br/Bz/CD/CL/CT/Cb/Cj/Cr=1-86. DR PDB; 4WZJ; X-ray; 3.60 A; AF/AM/AT/BF/BM/BT/CF/CM/CT/DF/DM/DT=1-86. DR PDB; 5MQF; EM; 5.90 A; b/i=1-86. DR PDB; 5O9Z; EM; 4.50 A; T/b/i=1-86. DR PDB; 5XJC; EM; 3.60 A; f/m=1-86. DR PDB; 5XJL; X-ray; 2.50 A; F=1-86. DR PDB; 5XJQ; X-ray; 3.28 A; F=1-86. DR PDB; 5XJR; X-ray; 3.12 A; F=1-86. DR PDB; 5XJS; X-ray; 3.38 A; F=1-86. DR PDB; 5XJT; X-ray; 2.92 A; F=1-86. DR PDB; 5XJU; X-ray; 2.58 A; F=1-86. DR PDB; 5YZG; EM; 4.10 A; f/m=1-86. DR PDB; 5Z56; EM; 5.10 A; f/m=1-86. DR PDB; 5Z57; EM; 6.50 A; f/m=1-86. DR PDB; 5Z58; EM; 4.90 A; f/m=1-86. DR PDB; 6AH0; EM; 5.70 A; Q/b/m=1-86. DR PDB; 6FF7; EM; 4.50 A; b/i=1-86. DR PDB; 6ICZ; EM; 3.00 A; f/m=1-86. DR PDB; 6ID0; EM; 2.90 A; f/m=1-86. DR PDB; 6ID1; EM; 2.86 A; f/m=1-86. DR PDB; 6QDV; EM; 3.30 A; f/q=4-75. DR PDB; 6QW6; EM; 2.92 A; 4f/5f=1-86. DR PDB; 6QX9; EM; 3.28 A; 1f/2f/4f/5f=1-86. DR PDB; 6V4X; EM; 3.20 A; F=1-86. DR PDB; 6Y53; EM; 7.10 A; i=1-86. DR PDB; 6Y5Q; EM; 7.10 A; i=1-86. DR PDB; 7A5P; EM; 5.00 A; f/i=1-86. DR PDB; 7ABG; EM; 7.80 A; b/i=1-86. DR PDB; 7ABI; EM; 8.00 A; b/i=1-86. DR PDB; 7B0Y; EM; 3.60 A; f=1-86. DR PDB; 7DVQ; EM; 2.89 A; f/m=1-86. DR PDB; 7EVO; EM; 2.50 A; b=1-86. DR PDB; 7QTT; EM; 3.10 A; h=1-86. DR PDB; 7VPX; EM; 3.00 A; b/m=1-86. DR PDB; 7W59; EM; 3.60 A; f/m=1-86. DR PDB; 7W5A; EM; 3.60 A; f/m=1-86. DR PDB; 7W5B; EM; 4.30 A; f/m=1-86. DR PDB; 8C6J; EM; 2.80 A; f/q=1-86. DR PDB; 8CH6; EM; 5.90 A; 2/h=1-86. DR PDB; 8HK1; EM; 2.70 A; b=1-86. DR PDB; 8QO9; EM; 5.29 A; 2f/4f/5f=1-86. DR PDBsum; 3CW1; -. DR PDBsum; 3JCR; -. DR PDBsum; 3PGW; -. DR PDBsum; 4F7U; -. DR PDBsum; 4PJO; -. DR PDBsum; 4V98; -. DR PDBsum; 4WZJ; -. DR PDBsum; 5MQF; -. DR PDBsum; 5O9Z; -. DR PDBsum; 5XJC; -. DR PDBsum; 5XJL; -. DR PDBsum; 5XJQ; -. DR PDBsum; 5XJR; -. DR PDBsum; 5XJS; -. DR PDBsum; 5XJT; -. DR PDBsum; 5XJU; -. DR PDBsum; 5YZG; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6AH0; -. DR PDBsum; 6FF7; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6ID0; -. DR PDBsum; 6ID1; -. DR PDBsum; 6QDV; -. DR PDBsum; 6QW6; -. DR PDBsum; 6QX9; -. DR PDBsum; 6V4X; -. DR PDBsum; 6Y53; -. DR PDBsum; 6Y5Q; -. DR PDBsum; 7A5P; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABI; -. DR PDBsum; 7B0Y; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7EVO; -. DR PDBsum; 7QTT; -. DR PDBsum; 7VPX; -. DR PDBsum; 7W59; -. DR PDBsum; 7W5A; -. DR PDBsum; 7W5B; -. DR PDBsum; 8C6J; -. DR PDBsum; 8CH6; -. DR PDBsum; 8HK1; -. DR PDBsum; 8QO9; -. DR AlphaFoldDB; P62306; -. DR EMDB; EMD-10689; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-11972; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-21050; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-31334; -. DR EMDB; EMD-32074; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-34841; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; P62306; -. DR BioGRID; 112520; 375. DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2705; U7 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-6033; Sm complex. DR CORUM; P62306; -. DR DIP; DIP-31221N; -. DR IntAct; P62306; 138. DR MINT; P62306; -. DR STRING; 9606.ENSP00000266735; -. DR GlyGen; P62306; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P62306; -. DR PhosphoSitePlus; P62306; -. DR SwissPalm; P62306; -. DR BioMuta; SNRPF; -. DR DMDM; 61237391; -. DR EPD; P62306; -. DR jPOST; P62306; -. DR MassIVE; P62306; -. DR MaxQB; P62306; -. DR PaxDb; 9606-ENSP00000266735; -. DR PeptideAtlas; P62306; -. DR ProteomicsDB; 57387; -. DR Pumba; P62306; -. DR TopDownProteomics; P62306; -. DR Antibodypedia; 17610; 119 antibodies from 24 providers. DR DNASU; 6636; -. DR Ensembl; ENST00000266735.10; ENSP00000266735.5; ENSG00000139343.11. DR GeneID; 6636; -. DR KEGG; hsa:6636; -. DR MANE-Select; ENST00000266735.10; ENSP00000266735.5; NM_003095.5; NP_003086.1. DR UCSC; uc001tej.5; human. DR AGR; HGNC:11162; -. DR CTD; 6636; -. DR DisGeNET; 6636; -. DR GeneCards; SNRPF; -. DR HGNC; HGNC:11162; SNRPF. DR HPA; ENSG00000139343; Low tissue specificity. DR MIM; 603541; gene. DR neXtProt; NX_P62306; -. DR OpenTargets; ENSG00000139343; -. DR PharmGKB; PA36003; -. DR VEuPathDB; HostDB:ENSG00000139343; -. DR eggNOG; KOG3482; Eukaryota. DR GeneTree; ENSGT00940000154818; -. DR HOGENOM; CLU_076902_12_1_1; -. DR InParanoid; P62306; -. DR OMA; HEYKGYL; -. DR OrthoDB; 20767at2759; -. DR PhylomeDB; P62306; -. DR TreeFam; TF314481; -. DR PathwayCommons; P62306; -. DR Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs. DR Reactome; R-HSA-191859; snRNP Assembly. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination. DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs. DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery. DR SignaLink; P62306; -. DR SIGNOR; P62306; -. DR BioGRID-ORCS; 6636; 841 hits in 1127 CRISPR screens. DR ChiTaRS; SNRPF; human. DR EvolutionaryTrace; P62306; -. DR GeneWiki; Small_nuclear_ribonucleoprotein_polypeptide_F; -. DR GenomeRNAi; 6636; -. DR Pharos; P62306; Tbio. DR PRO; PR:P62306; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P62306; Protein. DR Bgee; ENSG00000139343; Expressed in endometrium epithelium and 202 other cell types or tissues. DR ExpressionAtlas; P62306; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0034709; C:methylosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0034715; C:pICln-Sm protein complex; IDA:UniProtKB. DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; IDA:UniProtKB. DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB. DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005686; C:U2 snRNP; NAS:ComplexPortal. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005687; C:U4 snRNP; IDA:UniProtKB. DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:UniProtKB. DR GO; GO:0005682; C:U5 snRNP; NAS:ComplexPortal. DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB. DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; NAS:ComplexPortal. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IMP:UniProtKB. DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB. DR GO; GO:1903241; P:U2-type prespliceosome assembly; NAS:ComplexPortal. DR CDD; cd01722; Sm_F; 1. DR Gene3D; 2.30.30.100; -; 1. DR IDEAL; IID00157; -. DR InterPro; IPR016487; Lsm6/sSmF. DR InterPro; IPR010920; LSM_dom_sf. DR InterPro; IPR047575; Sm. DR InterPro; IPR001163; Sm_dom_euk/arc. DR InterPro; IPR034100; Sm_F. DR PANTHER; PTHR11021:SF0; SMALL NUCLEAR RIBONUCLEOPROTEIN F; 1. DR PANTHER; PTHR11021; SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F; 1. DR Pfam; PF01423; LSM; 1. DR PIRSF; PIRSF006609; snRNP_SmF; 1. DR SMART; SM00651; Sm; 1. DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1. DR PROSITE; PS52002; SM; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; KW Ribonucleoprotein; RNA-binding; Spliceosome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6" FT CHAIN 2..86 FT /note="Small nuclear ribonucleoprotein F" FT /id="PRO_0000125536" FT DOMAIN 6..78 FT /note="Sm" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|Ref.6" FT CONFLICT 86 FT /note="E -> D (in Ref. 2; CAG33032)" FT /evidence="ECO:0000305" FT HELIX 7..14 FT /evidence="ECO:0007829|PDB:5XJL" FT STRAND 17..23 FT /evidence="ECO:0007829|PDB:5XJL" FT STRAND 28..36 FT /evidence="ECO:0007829|PDB:5XJL" FT STRAND 42..51 FT /evidence="ECO:0007829|PDB:5XJL" FT STRAND 54..64 FT /evidence="ECO:0007829|PDB:5XJL" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:5XJL" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:5XJL" SQ SEQUENCE 86 AA; 9725 MW; 416B88D575DAE58A CRC64; MSLPLNPKPF LNGLTGKPVM VKLKWGMEYK GYLVSVDGYM NMQLANTEEY IDGALSGHLG EVLIRCNNVL YIRGVEEEEE DGEMRE //