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Database: UniProt
Entry: P62306
LinkDB: P62306
Original site: P62306 
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-SEP-2021, entry version 164.
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 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., 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).
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:28502770, PubMed:28781166, PubMed:28076346).
CC       Component of 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 minor U12
CC       spliceosome (PubMed:15146077). As part of the U7 snRNP it is involved
CC       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 small
CC       nuclear ribonucleoproteins (snRNPs), the building blocks of the
CC       spliceosome (PubMed:11991638, PubMed:19325628, PubMed:21516107,
CC       PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166,
CC       PubMed:28076346). Most spliceosomal snRNPs contain a common set of Sm
CC       proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that
CC       assemble in a heptameric protein ring on the Sm site of the small
CC       nuclear RNA to form the core snRNP (PubMed:19325628, PubMed:21516107,
CC       PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166,
CC       PubMed:28076346). Component of the U1 snRNP (PubMed:19325628,
CC       PubMed:25555158). The U1 snRNP is composed of the U1 snRNA and the 7
CC       core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG,
CC       and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-
CC       A and SNRPC/U1-C (PubMed:19325628, PubMed:25555158). Component of the
CC       U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC       least 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 SNRPG;
CC       the complex does not contain SNRPD1 and SNRPD2 (PubMed:11574479).
CC       Component of the U11/U12 snRNPs that are part of the U12-type
CC       spliceosome (PubMed:15146077). Part of the SMN-Sm complex that contains
CC       SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7,
CC       GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC       SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly
CC       (PubMed:18984161, PubMed:16314521). Forms a 6S pICln-Sm complex
CC       composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-
CC       like structure where CLNS1A/pICln mimics additional Sm proteins and
CC       which is unable to assemble into the core snRNP (PubMed:18984161,
CC       PubMed:23333303). Interacts with GEMIN2 (via N-terminus); the
CC       interaction is direct (PubMed:21816274, PubMed:31799625). Interacts
CC       with SNRPD2; the interaction is direct (PubMed:21816274,
CC       PubMed:31799625). Interacts with SNRPE; the interaction is direct
CC       (PubMed:21816274, 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   -!- 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}.
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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   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   SMR; P62306; -.
DR   BioGRID; 112520; 208.
DR   ComplexPortal; CPX-6033; Sm complex.
DR   CORUM; P62306; -.
DR   DIP; DIP-31221N; -.
DR   IntAct; P62306; 132.
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   BioMuta; SNRPF; -.
DR   DMDM; 61237391; -.
DR   EPD; P62306; -.
DR   jPOST; P62306; -.
DR   MassIVE; P62306; -.
DR   MaxQB; P62306; -.
DR   PaxDb; P62306; -.
DR   PeptideAtlas; P62306; -.
DR   PRIDE; P62306; -.
DR   ProteomicsDB; 57387; -.
DR   TopDownProteomics; P62306; -.
DR   Antibodypedia; 17610; 110 antibodies.
DR   DNASU; 6636; -.
DR   Ensembl; ENST00000266735; ENSP00000266735; ENSG00000139343.
DR   GeneID; 6636; -.
DR   KEGG; hsa:6636; -.
DR   UCSC; uc001tej.5; human.
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; ENSGT00940000164757; -.
DR   HOGENOM; CLU_076902_12_1_1; -.
DR   InParanoid; P62306; -.
DR   OMA; VKLKWGH; -.
DR   OrthoDB; 1534116at2759; -.
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   BioGRID-ORCS; 6636; 803 hits in 987 CRISPR screens.
DR   ChiTaRS; SNRPF; human.
DR   EvolutionaryTrace; P62306; -.
DR   GeneWiki; Small_nuclear_ribonucleoprotein_polypeptide_F; -.
DR   GenomeRNAi; 6636; -.
DR   Pharos; P62306; Tdark.
DR   PRO; PR:P62306; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P62306; protein.
DR   Bgee; ENSG00000139343; Expressed in oocyte and 234 other tissues.
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: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: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   CDD; cd01722; Sm_F; 1.
DR   IDEAL; IID00157; -.
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   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; SSF50182; 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   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
//
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