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Database: UniProt
Entry: P62304
LinkDB: P62304
Original site: P62304 
ID   RUXE_HUMAN              Reviewed;          92 AA.
AC   P62304; B2R5B9; P08578; Q15498; Q5BKT2;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   29-SEP-2021, entry version 169.
DE   RecName: Full=Small nuclear ribonucleoprotein E;
DE            Short=snRNP-E;
DE   AltName: Full=Sm protein E;
DE            Short=Sm-E;
DE            Short=SmE;
GN   Name=SNRPE;
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].
RX   PubMed=2974536; DOI=10.1093/nar/16.22.10593;
RA   Stanford D.R., Kehl M., Perry C.A., Holicky E., Harvey S.E., Rohleder A.M.,
RA   Rehder K., Luehrmann R., Wieben E.D.;
RT   "The complete primary structure of the human snRNP E protein.";
RL   Nucleic Acids Res. 16:10593-10605(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2972723;
RA   Stanford D.R., Perry C.A., Holicky E., Rohleder A.M., Wieben E.D.;
RT   "The small nuclear ribonucleoprotein E protein gene contains four introns
RT   and has upstream similarities to genes for ribosomal proteins.";
RL   J. Biol. Chem. 263:17772-17779(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
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=Lung, and Uterus;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-92.
RX   PubMed=2440864;
RA   Stanford D.R., Rohleder A., Neiswanger K., Wieben E.D.;
RT   "DNA sequence of a human Sm autoimmune antigen. The multigene family
RT   contains a processed pseudogene.";
RL   J. Biol. Chem. 262:9931-9934(1987).
RN   [7]
RP   INTERACTION WITH SMN1.
RX   PubMed=10500148; DOI=10.1073/pnas.96.20.11167;
RA   Pellizzoni L., Charroux B., Dreyfuss G.;
RT   "SMN mutants of spinal muscular atrophy patients are defective in binding
RT   to snRNP proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11167-11172(1999).
RN   [8]
RP   IDENTIFICATION IN THE U7 SNRNP COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
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   [9]
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   [10]
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   [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   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT HYPT11
RP   SER-45, AND CHARACTERIZATION OF VARIANT HYPT11 SER-45.
RX   PubMed=23246290; DOI=10.1016/j.ajhg.2012.10.022;
RA   Pasternack S.M., Refke M., Paknia E., Hennies H.C., Franz T., Schaefer N.,
RA   Fryer A., van Steensel M., Sweeney E., Just M., Grimm C., Kruse R.,
RA   Ferrandiz C., Noethen M.M., Fischer U., Betz R.C.;
RT   "Mutations in SNRPE, which encodes a core protein of the spliceosome, cause
RT   autosomal-dominant hypotrichosis simplex.";
RL   Am. J. Hum. Genet. 92:81-87(2013).
RN   [16]
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   [17]
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   [18] {ECO:0007744|PDB:5XJL}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SNRPD1; SNRPD2;
RP   SNRPF; SNRPG; SMN1 AND GEMIN2, AND INTERACTION WITH GEMIN2; SNRPF AND
RP   SNRPG.
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   [19]
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   [20]
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   [21] {ECO:0007744|PDB:4PJO}
RP   X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS), 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   [22] {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   [23] {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   [24] {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   [25] {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   [26] {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; SNRPF; SNRPG AND SMN1, AND INTERACTION WITH GEMIN2; SNRPG AND
RP   SNRPF.
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:23246290, PubMed:19325628, PubMed:23333303,
CC       PubMed:25555158, PubMed:26912367, PubMed:28502770, PubMed:28781166,
CC       PubMed:28076346). Component of both the pre-catalytic spliceosome B
CC       complex and activated spliceosome C complexes (PubMed:11991638,
CC       PubMed:28502770, PubMed:28781166, PubMed:28076346). Is also a component
CC       of the 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:23246290,
CC       ECO:0000269|PubMed:23333303, ECO:0000269|PubMed:25555158,
CC       ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, 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:23246290, PubMed:19325628,
CC       PubMed:21516107, PubMed:25555158, PubMed:26912367, PubMed:28502770,
CC       PubMed:28781166, PubMed:28076346). Most spliceosomal snRNPs contain a
CC       common set of Sm proteins, SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF
CC       and SNRPG that assemble in a heptameric protein ring on the Sm site of
CC       the small nuclear RNA to form the core snRNP (PubMed:19325628,
CC       PubMed:21516107, 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 the U1
CC       snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC       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 U11/U12
CC       snRNPs that are part of the U12-type spliceosome (PubMed:15146077).
CC       Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1,
CC       DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and
CC       the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG;
CC       catalyzes core snRNPs assembly (PubMed:18984161, PubMed:16314521).
CC       Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2,
CC       SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics
CC       additional Sm proteins and which is unable to assemble into the core
CC       snRNP (PubMed:18984161, PubMed:23333303). Interacts with SMN1; the
CC       interaction is direct (PubMed:10500148). Interacts with GEMIN2 (via N-
CC       terminus); the interaction is direct (PubMed:21816274,
CC       PubMed:31799625). Interacts with SNRPF; the interaction is direct
CC       (PubMed:21816274, PubMed:31799625). Interacts with SNRPG; the
CC       interaction is direct (PubMed:21816274, PubMed:31799625).
CC       {ECO:0000269|PubMed:10500148, 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:23246290,
CC       ECO:0000269|PubMed:23333303, ECO:0000269|PubMed:25555158,
CC       ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166,
CC       ECO:0000269|PubMed:31799625}.
CC   -!- INTERACTION:
CC       P62304; Q8TEQ6: GEMIN5; NbExp=3; IntAct=EBI-348082, EBI-443630;
CC       P62304; Q8WXD5: GEMIN6; NbExp=2; IntAct=EBI-348082, EBI-752301;
CC       P62304; Q9Y333: LSM2; NbExp=3; IntAct=EBI-348082, EBI-347416;
CC       P62304; Q9Y4Y9: LSM5; NbExp=4; IntAct=EBI-348082, EBI-373007;
CC       P62304; Q15428: SF3A2; NbExp=2; IntAct=EBI-348082, EBI-2462271;
CC       P62304; P62306: SNRPF; NbExp=11; IntAct=EBI-348082, EBI-356900;
CC       P62304; P62308: SNRPG; NbExp=8; IntAct=EBI-348082, EBI-624585;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}.
CC       Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638,
CC       ECO:0000269|PubMed:23246290, ECO:0000269|PubMed:26912367,
CC       ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC       ECO:0000269|PubMed:28781166}. Note=SMN-mediated assembly into core
CC       snRNPs occurs in the cytosol before SMN-mediated transport to the
CC       nucleus to be included in spliceosomes. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. In scalp skin, it is present in
CC       the hair follicle, the epidermis, and the dermis.
CC       {ECO:0000269|PubMed:23246290}.
CC   -!- DISEASE: Hypotrichosis 11 (HYPT11) [MIM:615059]: A form of
CC       hypotrichosis, a condition characterized by the presence of less than
CC       the normal amount of hair and abnormal hair follicles and shafts, which
CC       are thin and atrophic. The extent of scalp and body hair involvement
CC       can be very variable, within as well as between families. HYPT11 is an
CC       autosomal dominant form characterized by scanty or absent eyebrows and
CC       a highly variable degree of alopecia since birth, ranging from slight
CC       thinning of scalp and axillary hair to complete loss of scalp and body
CC       hair. Pubic hair remains mainly unaffected.
CC       {ECO:0000269|PubMed:23246290}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Patients with systemic lupus erythematosus produce
CC       antibodies which interact with snRNP proteins.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. {ECO:0000305}.
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DR   EMBL; M37716; AAA90926.1; -; mRNA.
DR   EMBL; M15919; AAA36621.1; -; mRNA.
DR   EMBL; X12466; CAA31007.1; -; mRNA.
DR   EMBL; AK312130; BAG35066.1; -; mRNA.
DR   EMBL; CH471067; EAW91494.1; -; Genomic_DNA.
DR   EMBL; BC002639; AAH02639.1; -; mRNA.
DR   EMBL; BC090951; AAH90951.1; -; mRNA.
DR   EMBL; M21258; AAB59365.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M21253; AAB59365.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS30979.1; -.
DR   PIR; A32127; A32127.
DR   RefSeq; NP_001291393.1; NM_001304464.1.
DR   RefSeq; NP_001315566.1; NM_001328637.1.
DR   RefSeq; NP_001315567.1; NM_001328638.1.
DR   RefSeq; NP_003085.1; NM_003094.3.
DR   PDB; 3CW1; X-ray; 5.49 A; E/W/X/Y=1-92.
DR   PDB; 3JCR; EM; 7.00 A; S/s=1-92.
DR   PDB; 3PGW; X-ray; 4.40 A; E/H=1-92.
DR   PDB; 4F7U; X-ray; 1.90 A; E/H=1-92.
DR   PDB; 4PJO; X-ray; 3.30 A; E/S/e/s=1-92.
DR   PDB; 4V98; X-ray; 3.10 A; AC/AK/AS/Aa/Ai/Aq/Ay/BC/BK/BS/Ba/Bi/Bq/By/CC/CK/CS/Ca/Ci/Cq=1-92.
DR   PDB; 4WZJ; X-ray; 3.60 A; AE/AL/AS/BE/BL/BS/CE/CL/CS/DE/DL/DS=1-92.
DR   PDB; 5MQF; EM; 5.90 A; c/j=1-92.
DR   PDB; 5O9Z; EM; 4.50 A; U/c/j=1-92.
DR   PDB; 5XJC; EM; 3.60 A; e/l=1-92.
DR   PDB; 5XJL; X-ray; 2.50 A; E=1-92.
DR   PDB; 5XJQ; X-ray; 3.28 A; E=1-92.
DR   PDB; 5XJR; X-ray; 3.12 A; E=1-92.
DR   PDB; 5XJS; X-ray; 3.38 A; E=1-92.
DR   PDB; 5XJT; X-ray; 2.92 A; E=1-92.
DR   PDB; 5XJU; X-ray; 2.58 A; E=1-92.
DR   PDB; 5YZG; EM; 4.10 A; e/l=1-92.
DR   PDB; 5Z56; EM; 5.10 A; e/l=1-92.
DR   PDB; 5Z57; EM; 6.50 A; e/l=1-92.
DR   PDB; 5Z58; EM; 4.90 A; e/l=1-92.
DR   PDB; 6AH0; EM; 5.70 A; R/c/l=1-92.
DR   PDB; 6FF7; EM; 4.50 A; c/j=1-92.
DR   PDB; 6ICZ; EM; 3.00 A; e/l=1-92.
DR   PDB; 6ID0; EM; 2.90 A; e/l=1-92.
DR   PDB; 6ID1; EM; 2.86 A; e/l=1-92.
DR   PDB; 6QDV; EM; 3.30 A; e/p=11-91.
DR   PDB; 6QW6; EM; 2.92 A; 4e/5e=1-92.
DR   PDB; 6QX9; EM; 3.28 A; 1e/2e/4e/5e=1-92.
DR   PDB; 6V4X; EM; 3.20 A; E=1-92.
DR   PDB; 6Y53; EM; 7.10 A; j=1-92.
DR   PDB; 6Y5Q; EM; 7.10 A; j=1-92.
DR   PDB; 7A5P; EM; 5.00 A; e/j=1-92.
DR   PDB; 7ABG; EM; 7.80 A; c/j=1-92.
DR   PDB; 7ABI; EM; 8.00 A; c/j=1-92.
DR   PDB; 7B0Y; EM; 3.60 A; g=1-92.
DR   PDB; 7DVQ; EM; 2.89 A; e/l=1-92.
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; P62304; -.
DR   BioGRID; 112519; 216.
DR   ComplexPortal; CPX-6033; Sm complex.
DR   CORUM; P62304; -.
DR   DIP; DIP-31220N; -.
DR   IntAct; P62304; 149.
DR   MINT; P62304; -.
DR   STRING; 9606.ENSP00000400591; -.
DR   GlyGen; P62304; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P62304; -.
DR   MetOSite; P62304; -.
DR   PhosphoSitePlus; P62304; -.
DR   SwissPalm; P62304; -.
DR   BioMuta; SNRPE; -.
DR   DMDM; 61237380; -.
DR   EPD; P62304; -.
DR   jPOST; P62304; -.
DR   MassIVE; P62304; -.
DR   MaxQB; P62304; -.
DR   PaxDb; P62304; -.
DR   PeptideAtlas; P62304; -.
DR   PRIDE; P62304; -.
DR   ProteomicsDB; 57386; -.
DR   TopDownProteomics; P62304; -.
DR   Antibodypedia; 53843; 207 antibodies.
DR   DNASU; 6635; -.
DR   Ensembl; ENST00000414487; ENSP00000400591; ENSG00000182004.
DR   GeneID; 6635; -.
DR   KEGG; hsa:6635; -.
DR   UCSC; uc001hai.4; human.
DR   CTD; 6635; -.
DR   DisGeNET; 6635; -.
DR   GeneCards; SNRPE; -.
DR   HGNC; HGNC:11161; SNRPE.
DR   HPA; ENSG00000182004; Low tissue specificity.
DR   MalaCards; SNRPE; -.
DR   MIM; 128260; gene.
DR   MIM; 615059; phenotype.
DR   neXtProt; NX_P62304; -.
DR   OpenTargets; ENSG00000182004; -.
DR   Orphanet; 55654; Hypotrichosis simplex.
DR   PharmGKB; PA36002; -.
DR   VEuPathDB; HostDB:ENSG00000182004; -.
DR   eggNOG; KOG1774; Eukaryota.
DR   GeneTree; ENSGT00390000012818; -.
DR   HOGENOM; CLU_125186_1_0_1; -.
DR   InParanoid; P62304; -.
DR   OMA; QIWLYED; -.
DR   OrthoDB; 1594132at2759; -.
DR   PhylomeDB; P62304; -.
DR   TreeFam; TF314419; -.
DR   PathwayCommons; P62304; -.
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; 6635; 745 hits in 975 CRISPR screens.
DR   ChiTaRS; SNRPE; human.
DR   EvolutionaryTrace; P62304; -.
DR   GenomeRNAi; 6635; -.
DR   Pharos; P62304; Tbio.
DR   PRO; PR:P62304; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P62304; protein.
DR   Bgee; ENSG00000182004; Expressed in subventricular zone (inner) (primate) and 136 other tissues.
DR   ExpressionAtlas; P62304; baseline and differential.
DR   Genevisible; P62304; 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:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR   GO; GO:0030532; C:small nuclear ribonucleoprotein complex; NAS:UniProtKB.
DR   GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB.
DR   GO; GO:0005697; C:telomerase holoenzyme complex; IDA:BHF-UCL.
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; IBA:GO_Central.
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:0005682; C:U5 snRNP; IBA:GO_Central.
DR   GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042633; P:hair cycle; IMP:UniProtKB.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0000245; P:spliceosomal complex assembly; NAS:UniProtKB.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR   CDD; cd01718; Sm_E; 1.
DR   IDEAL; IID00156; -.
DR   InterPro; IPR001163; LSM_dom_euk/arc.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR027078; snRNP-E.
DR   PANTHER; PTHR11193; PTHR11193; 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; Cytoplasm; Disease variant; Hypotrichosis; mRNA processing;
KW   mRNA splicing; Nucleus; Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Spliceosome.
FT   CHAIN           1..92
FT                   /note="Small nuclear ribonucleoprotein E"
FT                   /id="PRO_0000125529"
FT   VARIANT         45
FT                   /note="G -> S (in HYPT11; does not affect subcellular
FT                   localization; dbSNP:rs587776925)"
FT                   /evidence="ECO:0000269|PubMed:23246290"
FT                   /id="VAR_069619"
FT   HELIX           17..27
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          30..37
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          39..50
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          56..68
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          71..79
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   HELIX           81..83
FT                   /evidence="ECO:0007829|PDB:5XJL"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:5XJL"
SQ   SEQUENCE   92 AA;  10804 MW;  7D8881CE1F4FA2FD CRC64;
     MAYRGQGQKV QKVMVQPINL IFRYLQNRSR IQVWLYEQVN MRIEGCIIGF DEYMNLVLDD
     AEEIHSKTKS RKQLGRIMLK GDNITLLQSV SN
//
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