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 01-APR-2015, entry version 110. 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. 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, AND IDENTIFICATION IN THE RP SPLICEOSOMAL C COMPLEX. 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 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 [10] 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 [11] 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 [12] 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 [13] RP X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) IN SPLICEOSOMAL U1 SNRNP. 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 [14] RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP. 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 [15] 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). CC -!- FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5 CC small nuclear ribonucleoproteins (snRNPs), the building blocks of CC the spliceosome. Thereby, plays an important role in the splicing CC of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common CC set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and CC SNRPG that assemble in an heptameric protein ring on the Sm site CC of the small nuclear RNA to form the core snRNP. As part of the U7 CC snRNP it is involved in histone 3'-end processing. CC {ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:23333303}. CC -!- SUBUNIT: U1 snRNP is for instance composed of the 7 core Sm CC proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG CC that assemble in an heptameric protein ring on the Sm site of the CC small nuclear RNA to form the core snRNP, and at least three U1 CC snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. CC Component of the U11/U12 snRNPs that are part of the U12-type CC spliceosome. Component of the heptameric ring U7 snRNP complex, or CC U7 Sm protein core complex, at least composed of LSM10, LSM11, CC SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Part of the SMN- CC Sm 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. Forms a 6S pICln-Sm complex composed of CC CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like CC structure where CLNS1A/pICln mimics additional Sm proteins and CC which is unable to assemble into the core snRNP. CC {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:18984161, CC ECO:0000269|PubMed:23333303}. CC -!- INTERACTION: CC P54105:CLNS1A; NbExp=4; IntAct=EBI-356900, EBI-724693; CC P62304:SNRPE; NbExp=4; IntAct=EBI-356900, EBI-348082; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000269|PubMed:18984161}. Nucleus CC {ECO:0000269|PubMed:18984161}. Note=SMN-mediated assembly into CC core snRNPs occurs in the cytosol before SMN-mediated transport to CC the nucleus to be included in spliceosomes. 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; 3PGW; X-ray; 4.40 A; F/I=1-86. DR PDB; 3S6N; X-ray; 2.50 A; F=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 PDBsum; 3CW1; -. DR PDBsum; 3PGW; -. DR PDBsum; 3S6N; -. DR PDBsum; 4F7U; -. DR PDBsum; 4PJO; -. DR PDBsum; 4V98; -. DR PDBsum; 4WZJ; -. DR ProteinModelPortal; P62306; -. DR SMR; P62306; 3-76. DR BioGrid; 112520; 71. DR DIP; DIP-31221N; -. DR IntAct; P62306; 28. DR MINT; MINT-1137229; -. DR STRING; 9606.ENSP00000266735; -. DR PhosphoSite; P62306; -. DR DMDM; 61237391; -. DR MaxQB; P62306; -. DR PaxDb; P62306; -. DR PeptideAtlas; P62306; -. DR PRIDE; P62306; -. DR Ensembl; ENST00000266735; ENSP00000266735; ENSG00000139343. DR GeneID; 6636; -. DR KEGG; hsa:6636; -. DR UCSC; uc001tej.3; human. DR CTD; 6636; -. DR GeneCards; GC12P096252; -. DR HGNC; HGNC:11162; SNRPF. DR MIM; 603541; gene. DR neXtProt; NX_P62306; -. DR PharmGKB; PA36003; -. DR eggNOG; COG1958; -. DR GeneTree; ENSGT00730000110856; -. DR HOVERGEN; HBG052369; -. DR InParanoid; P62306; -. DR KO; K11098; -. DR OMA; STDGYMN; -. DR OrthoDB; EOG7HXCTK; -. DR PhylomeDB; P62306; -. DR TreeFam; TF314481; -. DR Reactome; REACT_11066; snRNP Assembly. DR Reactome; REACT_1364; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs. DR Reactome; REACT_1753; mRNA Splicing - Minor Pathway. DR Reactome; REACT_185; SLBP independent Processing of Histone Pre-mRNAs. DR Reactome; REACT_387; Cleavage of Growing Transcript in the Termination Region. DR Reactome; REACT_467; mRNA Splicing - Major Pathway. DR ChiTaRS; SNRPF; human. DR EvolutionaryTrace; P62306; -. DR GeneWiki; Small_nuclear_ribonucleoprotein_polypeptide_F; -. DR GenomeRNAi; 6636; -. DR NextBio; 25853; -. DR PMAP-CutDB; P62306; -. DR PRO; PR:P62306; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; P62306; -. DR CleanEx; HS_SNRPF; -. DR ExpressionAtlas; P62306; baseline and differential. DR Genevestigator; P62306; -. 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: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:0005687; C:U4 snRNP; IDA:UniProtKB. DR GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IMP:UniProtKB. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome. DR GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB. DR GO; GO:0034660; P:ncRNA metabolic process; TAS:Reactome. 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 GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:Reactome. DR InterPro; IPR016487; Lsm6/sSmF. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR001163; Ribonucl_LSM. DR InterPro; IPR006649; Ribonucl_LSM_euk/arc. 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:3S6N}. FT STRAND 17 23 {ECO:0000244|PDB:3S6N}. FT STRAND 28 36 {ECO:0000244|PDB:3S6N}. FT STRAND 42 51 {ECO:0000244|PDB:3S6N}. FT STRAND 54 64 {ECO:0000244|PDB:3S6N}. FT HELIX 66 68 {ECO:0000244|PDB:3S6N}. FT STRAND 69 74 {ECO:0000244|PDB:3S6N}. SQ SEQUENCE 86 AA; 9725 MW; 416B88D575DAE58A CRC64; MSLPLNPKPF LNGLTGKPVM VKLKWGMEYK GYLVSVDGYM NMQLANTEEY IDGALSGHLG EVLIRCNNVL YIRGVEEEEE DGEMRE //