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 16-JAN-2019, entry version 146. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Cervix carcinoma; RX PubMed=7744013; 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 RT which 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RP 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, RT a new 14 kDa Sm D1-like protein."; RL EMBO J. 20:5470-5479(2001). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RP SPLICEOSOMAL C 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., RA Fischer U., 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., RA Mann M.; RT "Proteomic characterization of the human centrosome by protein RT correlation profiling."; RL Nature 426:570-574(2003). RN [11] RP IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15146077; DOI=10.1261/rna.7320604; RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., RA Elbashir S., Tuschl T., Luehrmann R.; RT "The human 18S U11/U12 snRNP contains a set of novel proteins not RT found in the U2-dependent spliceosome."; RL RNA 10:929-941(2004). RN [12] 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 [13] 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., RA Buerckstuemmer T., 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 [14] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP, RP FUNCTION, 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 RT resolution."; RL Nature 458:475-480(2009). RN [16] RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP, RP AND 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 RT implication for snRNP biogenesis."; RL Nature 473:536-539(2011). RN [17] 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 [18] {ECO:0000244|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 RT ribonucleoprotein particle, reveals the mechanism of 5' splice site RT recognition."; RL Elife 4:0-0(2015). RN [19] {ECO:0000244|PDB:3JCR} RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBCELLULAR RP LOCATION, 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., RA Urlaub H., Luhrmann R., Stark H.; RT "Molecular architecture of the human U4/U6.U5 tri-snRNP."; RL Science 351:1416-1420(2016). RN [20] {ECO:0000244|PDB:5XJC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, RP SUBCELLULAR 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 [21] {ECO:0000244|PDB:5O9Z} RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, RP SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS RP 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 [22] {ECO:0000244|PDB:5MQF} RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, RP SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=28076346; DOI=10.1038/nature21079; RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., RA Hartmuth K., 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). CC -!- FUNCTION: Plays role in pre-mRNA splicing as core component of the CC SMN-Sm complex that mediates spliceosomal snRNP assembly and as CC component of the spliceosomal U1, U2, U4 and U5 small nuclear CC ribonucleoproteins (snRNPs), the building blocks of the CC spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, CC PubMed:23333303, PubMed:25555158, PubMed:26912367, CC PubMed:28502770, PubMed:28781166, PubMed:28076346). Component of CC both the pre-catalytic spliceosome B complex and activated CC spliceosome C complexes (PubMed:11991638, PubMed:28502770, CC PubMed:28781166, PubMed:28076346). Is also a component of the CC minor U12 spliceosome (PubMed:15146077). As part of the U7 snRNP CC it is involved in 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}. CC -!- SUBUNIT: Core component of the spliceosomal U1, U2, U4 and U5 CC small nuclear ribonucleoproteins (snRNPs), the building blocks of CC the spliceosome (PubMed:11991638, PubMed:19325628, CC PubMed:21516107, PubMed:25555158, PubMed:26912367, CC PubMed:28502770, PubMed:28781166, PubMed:28076346). Most CC spliceosomal snRNPs contain a common set of Sm proteins, SNRPB, CC SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a CC heptameric protein ring on the Sm site of the small nuclear RNA to CC form the core snRNP (PubMed:19325628, PubMed:21516107, CC PubMed:25555158, PubMed:26912367, PubMed:28502770, CC PubMed:28781166, PubMed:28076346). Component of the U1 snRNP CC (PubMed:19325628, PubMed:25555158). The U1 snRNP is composed of CC the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, CC SNRPD3, SNRPE, SNRPF and SNRPG, and at least three U1 snRNP- CC specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C CC (PubMed:19325628, PubMed:25555158). Component of the U4/U6-U5 tri- CC snRNP complex composed of the U4, U6 and U5 snRNAs and at least CC PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, CC PPIH, SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, CC LSM6, LSM7 and LSM8 (PubMed:26912367). Component of the U7 snRNP CC complex, or U7 Sm protein core complex, that is composed of the U7 CC snRNA and at least LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and CC SNRPG; the complex does not contain SNRPD1 and SNRPD2 CC (PubMed:11574479). Component of the U11/U12 snRNPs that are part CC of the U12-type spliceosome (PubMed:15146077). Part of the SMN-Sm CC complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, CC GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes CC core snRNPs assembly (PubMed:18984161). Forms a 6S pICln-Sm CC complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and CC SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm CC proteins and which is unable to assemble into the core snRNP CC (PubMed:18984161, PubMed:23333303). {ECO:0000269|PubMed:11574479, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:15146077, CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:19325628, CC ECO:0000269|PubMed:21516107, 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}. CC -!- INTERACTION: CC P54105:CLNS1A; NbExp=4; IntAct=EBI-356900, EBI-724693; CC P38432:COIL; NbExp=5; IntAct=EBI-356900, EBI-945751; CC O14893:GEMIN2; NbExp=8; IntAct=EBI-356900, EBI-443648; CC Q9NSC5:HOMER3; NbExp=7; IntAct=EBI-356900, EBI-748420; CC Q13422:IKZF1; NbExp=3; IntAct=EBI-356900, EBI-745305; CC Q8TBB1:LNX1; NbExp=3; IntAct=EBI-356900, EBI-739832; CC Q9Y4Y9:LSM5; NbExp=10; IntAct=EBI-356900, EBI-373007; CC Q9UK45:LSM7; NbExp=3; IntAct=EBI-356900, EBI-348372; CC P62316:SNRPD2; NbExp=6; IntAct=EBI-356900, EBI-297993; CC P62304:SNRPE; NbExp=8; IntAct=EBI-356900, EBI-348082; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000269|PubMed:18984161}. Nucleus CC {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}. CC Note=SMN-mediated assembly into core snRNPs occurs in the cytosol CC before SMN-mediated transport to the nucleus to be included in CC spliceosomes. {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 UniGene; Hs.105465; -. 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 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 ProteinModelPortal; P62306; -. DR SMR; P62306; -. DR BioGrid; 112520; 157. DR CORUM; P62306; -. DR DIP; DIP-31221N; -. DR IntAct; P62306; 42. DR MINT; P62306; -. DR STRING; 9606.ENSP00000266735; -. DR iPTMnet; P62306; -. DR PhosphoSitePlus; P62306; -. DR BioMuta; SNRPF; -. DR DMDM; 61237391; -. DR EPD; P62306; -. DR jPOST; P62306; -. DR MaxQB; P62306; -. DR PaxDb; P62306; -. DR PeptideAtlas; P62306; -. DR PRIDE; P62306; -. DR ProteomicsDB; 57387; -. DR TopDownProteomics; P62306; -. DR Ensembl; ENST00000266735; ENSP00000266735; ENSG00000139343. DR GeneID; 6636; -. DR KEGG; hsa:6636; -. DR UCSC; uc001tej.5; human. DR CTD; 6636; -. DR DisGeNET; 6636; -. DR EuPathDB; HostDB:ENSG00000139343.10; -. DR GeneCards; SNRPF; -. DR HGNC; HGNC:11162; SNRPF. DR MIM; 603541; gene. DR neXtProt; NX_P62306; -. DR OpenTargets; ENSG00000139343; -. DR PharmGKB; PA36003; -. DR eggNOG; KOG3482; Eukaryota. DR eggNOG; ENOG4111W47; LUCA. DR GeneTree; ENSGT00940000154818; -. DR HOVERGEN; HBG052369; -. DR InParanoid; P62306; -. DR KO; K11098; -. DR OMA; VKLKWGH; -. DR OrthoDB; 1534116at2759; -. DR PhylomeDB; P62306; -. DR TreeFam; TF314481; -. DR Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region. 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-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs. DR ChiTaRS; SNRPF; human. DR EvolutionaryTrace; P62306; -. DR GeneWiki; Small_nuclear_ribonucleoprotein_polypeptide_F; -. DR GenomeRNAi; 6636; -. DR PMAP-CutDB; P62306; -. DR PRO; PR:P62306; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000139343; Expressed in 223 organ(s), highest expression level in oocyte. DR CleanEx; HS_SNRPF; -. DR ExpressionAtlas; P62306; baseline and differential. DR Genevisible; P62306; HS. 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:0005732; C:small nucleolar ribonucleoprotein complex; IEA:InterPro. 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:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; 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:0005683; C:U7 snRNP; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB. DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome. DR GO; GO:0051170; P:import into nucleus; TAS:Reactome. 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:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome. DR CDD; cd01722; Sm_F; 1. DR InterPro; IPR016487; Lsm6/sSmF. DR InterPro; IPR001163; LSM_dom_euk/arc. DR InterPro; IPR010920; LSM_dom_sf. DR InterPro; IPR034100; Sm_F. DR PANTHER; PTHR11021; PTHR11021; 1. DR Pfam; PF01423; LSM; 1. DR PIRSF; PIRSF006609; snRNP_SmF; 1. DR SMART; SM00651; Sm; 1. DR SUPFAM; SSF50182; SSF50182; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; KW Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus; KW Reference proteome; Ribonucleoprotein; RNA-binding; Spliceosome. FT INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}. FT CHAIN 2 86 Small nuclear ribonucleoprotein F. FT /FTId=PRO_0000125536. FT MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.6}. FT CONFLICT 86 86 E -> D (in Ref. 2; CAG33032). FT {ECO:0000305}. FT HELIX 7 14 {ECO:0000244|PDB:5XJL}. FT STRAND 17 23 {ECO:0000244|PDB:5XJL}. FT STRAND 28 36 {ECO:0000244|PDB:5XJL}. FT STRAND 42 51 {ECO:0000244|PDB:5XJL}. FT STRAND 54 64 {ECO:0000244|PDB:5XJL}. FT HELIX 66 68 {ECO:0000244|PDB:5XJL}. FT STRAND 69 74 {ECO:0000244|PDB:5XJL}. SQ SEQUENCE 86 AA; 9725 MW; 416B88D575DAE58A CRC64; MSLPLNPKPF LNGLTGKPVM VKLKWGMEYK GYLVSVDGYM NMQLANTEEY IDGALSGHLG EVLIRCNNVL YIRGVEEEEE DGEMRE //