RSMB_HUMAN
ID RSMB_HUMAN Reviewed; 240 AA.
AC P14678; Q15490; Q6IB35; Q9UIS5;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 2.
DT 03-AUG-2022, entry version 234.
DE RecName: Full=Small nuclear ribonucleoprotein-associated proteins B and B';
DE Short=snRNP-B;
DE AltName: Full=Sm protein B/B';
DE Short=Sm-B/B';
DE Short=SmB/B';
GN Name=SNRPB; Synonyms=COD, SNRPB1;
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] (ISOFORMS SM-B AND SM-B').
RX PubMed=2531083;
RA van Dam A., Winkel I., Zijlstra-Baalbergen J., Smeenk R., Cuypers H.T.;
RT "Cloned human snRNP proteins B and B' differ only in their carboxy-terminal
RT part.";
RL EMBO J. 8:3853-3860(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SM-B).
RC TISSUE=Thyroid carcinoma;
RX PubMed=2522186; DOI=10.1093/nar/17.4.1733;
RA Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.;
RT "A comparison of snRNP-associated Sm-autoantigens: human N, rat N and human
RT B/B'.";
RL Nucleic Acids Res. 17:1733-1743(1989).
RN [3]
RP ERRATUM OF PUBMED:2522186.
RA Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.;
RL Nucleic Acids Res. 17:6777-6777(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SM-B1).
RC TISSUE=Fibroblast;
RX PubMed=2524838; DOI=10.1073/pnas.86.11.4249;
RA Ohosone Y., Mimori T., Griffith A., Akizuki M., Homma M., Craft J.,
RA Hardin J.A.;
RT "Molecular cloning of cDNA encoding Sm autoantigen: derivation of a cDNA
RT for a B polypeptide of the U series of small nuclear ribonucleoprotein
RT particles.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:4249-4253(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10556313; DOI=10.1093/nar/27.23.4577;
RA Gray T.A., Smithwick M.J., Schaldach M.A., Martone D.L., Graves J.A.,
RA McCarrey J.R., Nicholls R.D.;
RT "Concerted regulation and molecular evolution of the duplicated SNRPB'/B
RT and SNRPN loci.";
RL Nucleic Acids Res. 27:4577-4584(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SM-B').
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-240 (ISOFORMS SM-B AND SM-B').
RX PubMed=1694885;
RA Elkon K.B., Hines J.J., Chu J.-L., Parnassa A.;
RT "Epitope mapping of recombinant HeLa SmB and B' peptides obtained by the
RT polymerase chain reaction.";
RL J. Immunol. 145:636-643(1990).
RN [10]
RP PROTEIN SEQUENCE OF 9-16; 19-32 AND 66-147, METHYLATION AT ARG-108; ARG-112
RP AND ARG-147, 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 [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 209-240.
RX PubMed=1825643; DOI=10.1016/0378-1119(91)90069-n;
RA Chu J.-L., Elkon K.B.;
RT "The small nuclear ribonucleoproteins, SmB and B', are products of a single
RT gene.";
RL Gene 97:311-312(1991).
RN [12]
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 [13]
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 [14]
RP INTERACTION WITH DDX20; SNUPN AND SMN1.
RX PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
RA Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
RT "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex
RT with snurportin1 and importin beta.";
RL Hum. Mol. Genet. 11:1785-1795(2002).
RN [15]
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 [16]
RP INTERACTION WITH LSM11, SUBUNIT, AND FUNCTION.
RC TISSUE=Cervix carcinoma;
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 [17]
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 [18]
RP INTERACTION WITH TDRD3.
RX PubMed=15955813; DOI=10.1074/jbc.m414328200;
RA Cote J., Richard S.;
RT "Tudor domains bind symmetrical dimethylated arginines.";
RL J. Biol. Chem. 280:28476-28483(2005).
RN [19]
RP INTERACTION WITH CLNS1A AND SMN, AND METHYLATION.
RX PubMed=16087681; DOI=10.1074/jbc.m505077200;
RA Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
RA Fischer U., Schuemperli D.;
RT "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm
RT proteins with PRMT5 and SMN complexes.";
RL J. Biol. Chem. 280:34435-34440(2005).
RN [20]
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 [21]
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 [22]
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 [23]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-108 AND ARG-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [24]
RP INVOLVEMENT IN CCMS, VARIANTS CCMS SER-55; ARG-56 AND TRP-56, AND
RP CHARACTERIZATION OF VARIANTS CCMS SER-55.
RX PubMed=25047197; DOI=10.1038/ncomms5483;
RG Care4Rare Canada;
RA Lynch D.C., Revil T., Schwartzentruber J., Bhoj E.J., Innes A.M.,
RA Lamont R.E., Lemire E.G., Chodirker B.N., Taylor J.P., Zackai E.H.,
RA McLeod D.R., Kirk E.P., Hoover-Fong J., Fleming L., Savarirayan R.,
RA Majewski J., Jerome-Majewska L.A., Parboosingh J.S., Bernier F.P.;
RT "Disrupted auto-regulation of the spliceosomal gene SNRPB causes cerebro-
RT costo-mandibular syndrome.";
RL Nat. Commun. 5:4483-4483(2014).
RN [25]
RP INVOLVEMENT IN CCMS, AND VARIANTS CCMS SER-55; THR-55 AND ARG-56.
RX PubMed=25504470; DOI=10.1002/humu.22729;
RA Bacrot S., Doyard M., Huber C., Alibeu O., Feldhahn N., Lehalle D.,
RA Lacombe D., Marlin S., Nitschke P., Petit F., Vazquez M.P., Munnich A.,
RA Cormier-Daire V.;
RT "Mutations in SNRPB, encoding components of the core splicing machinery,
RT cause cerebro-costo-mandibular syndrome.";
RL Hum. Mutat. 36:187-190(2015).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10025403; DOI=10.1016/s0092-8674(00)80550-4;
RA Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., Raker V.A.,
RA Luehrmann R., Li J., Nagai K.;
RT "Crystal structures of two Sm protein complexes and their implications for
RT the assembly of the spliceosomal snRNPs.";
RL Cell 96:375-387(1999).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-174 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 resolution.";
RL Nature 458:475-480(2009).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-95 IN SPLICEOSOMAL CORE U4
RP SNRNP, 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 implication for
RT snRNP biogenesis.";
RL Nature 473:536-539(2011).
RN [29] {ECO:0007744|PDB:4PJO}
RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 1-95, 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 [30] {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 [31] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 1-229, 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 [32] {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 [33] {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).
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:25555158, PubMed:26912367,
CC PubMed:28502770, PubMed:28781166, PubMed:28076346). Component of both
CC the pre-catalytic spliceosome B complex and activated spliceosome C
CC complexes (PubMed:11991638, PubMed:28502770, PubMed:28781166,
CC PubMed:28076346). Is also a component of the minor U12 spliceosome
CC (PubMed:15146077). As part of the U7 snRNP it is involved in histone
CC pre-mRNA 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: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:10025403, 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:10025403,
CC PubMed:19325628, PubMed:21516107, PubMed:25555158, PubMed:26912367,
CC PubMed:28502770, PubMed:28781166, PubMed:28076346). Component of the U1
CC snRNP (PubMed:19325628, PubMed:25555158). The U1 snRNP is composed of
CC the U1 snRNA and the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF and SNRPG, and at least three U1 snRNP-specific proteins
CC SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C (PubMed:19325628,
CC PubMed:25555158). Component of the U4/U6-U5 tri-snRNP complex composed
CC of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8,
CC PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB, SNRPD1, SNRPD2, SNRPD3,
CC SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and
CC USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8
CC (PubMed:26912367). Component of the U7 snRNP complex, or U7 Sm protein
CC core complex, that is composed of the U7 snRNA and at least LSM10,
CC LSM11, SNRPB, SNRPD3, SNRPE, SNRPF and SNRPG; the complex does not
CC contain SNRPD1 and SNRPD2 (PubMed:11574479, PubMed:12975319). Component
CC of the U11/U12 snRNPs that are part of the U12-type spliceosome
CC (PubMed:15146077). Part of the SMN-Sm complex that contains SMN1,
CC GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC SNRPF and SNRPG; catalyzes core snRNPs assembly (PubMed:12095920,
CC PubMed:18984161, PubMed:16314521). Forms a 6S pICln-Sm complex composed
CC of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like
CC structure where CLNS1A/pICln mimics additional Sm proteins and which is
CC unable to assemble into the core snRNP (PubMed:18984161). Identified in
CC a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
CC SNRPB, SYNCRIP and YBX1 (By similarity). Interacts with TDRD3 and SNUPN
CC (PubMed:12095920, PubMed:15955813). Interacts with PRMT5; interaction
CC leads to its symmetric arginine dimethylation (By similarity).
CC Interacts with TDRD6; interaction promotes association with PRMT5 (By
CC similarity). Interacts with SMN1; the interaction is direct
CC (PubMed:10500148). {ECO:0000250|UniProtKB:P27048,
CC ECO:0000269|PubMed:10025403, ECO:0000269|PubMed:11574479,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12095920,
CC ECO:0000269|PubMed:12975319, ECO:0000269|PubMed:15146077,
CC ECO:0000269|PubMed:15955813, ECO:0000269|PubMed:16087681,
CC ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:18984161,
CC ECO:0000269|PubMed:19325628, ECO:0000269|PubMed:21516107,
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 P14678; P54253: ATXN1; NbExp=3; IntAct=EBI-372458, EBI-930964;
CC P14678; O95400: CD2BP2; NbExp=8; IntAct=EBI-372458, EBI-768015;
CC P14678; P54105: CLNS1A; NbExp=3; IntAct=EBI-372458, EBI-724693;
CC P14678; P62318: SNRPD3; NbExp=4; IntAct=EBI-372458, EBI-372789;
CC P14678-1; Q16637-3: SMN2; NbExp=3; IntAct=EBI-372471, EBI-395447;
CC P14678-2; Q6PJH3: AKAP9; NbExp=3; IntAct=EBI-372475, EBI-11745576;
CC P14678-2; O95429: BAG4; NbExp=5; IntAct=EBI-372475, EBI-2949658;
CC P14678-2; Q8N9N5: BANP; NbExp=3; IntAct=EBI-372475, EBI-744695;
CC P14678-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-372475, EBI-11524452;
CC P14678-2; Q14457: BECN1; NbExp=3; IntAct=EBI-372475, EBI-949378;
CC P14678-2; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-372475, EBI-12809220;
CC P14678-2; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-372475, EBI-739580;
CC P14678-2; O95400: CD2BP2; NbExp=10; IntAct=EBI-372475, EBI-768015;
CC P14678-2; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-372475, EBI-747776;
CC P14678-2; P54105: CLNS1A; NbExp=3; IntAct=EBI-372475, EBI-724693;
CC P14678-2; Q96BR5: COA7; NbExp=3; IntAct=EBI-372475, EBI-6269632;
CC P14678-2; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-372475, EBI-3866319;
CC P14678-2; Q03060-25: CREM; NbExp=3; IntAct=EBI-372475, EBI-12884642;
CC P14678-2; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-372475, EBI-2872414;
CC P14678-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-372475, EBI-3867333;
CC P14678-2; O75553: DAB1; NbExp=3; IntAct=EBI-372475, EBI-7875264;
CC P14678-2; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-372475, EBI-21529239;
CC P14678-2; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-372475, EBI-371922;
CC P14678-2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-372475, EBI-12193763;
CC P14678-2; Q13643: FHL3; NbExp=3; IntAct=EBI-372475, EBI-741101;
CC P14678-2; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-372475, EBI-12121668;
CC P14678-2; O75420: GIGYF1; NbExp=3; IntAct=EBI-372475, EBI-947774;
CC P14678-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-372475, EBI-618309;
CC P14678-2; P31943: HNRNPH1; NbExp=3; IntAct=EBI-372475, EBI-351590;
CC P14678-2; P49639: HOXA1; NbExp=3; IntAct=EBI-372475, EBI-740785;
CC P14678-2; Q0VD86: INCA1; NbExp=3; IntAct=EBI-372475, EBI-6509505;
CC P14678-2; O76011: KRT34; NbExp=3; IntAct=EBI-372475, EBI-1047093;
CC P14678-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-372475, EBI-10171697;
CC P14678-2; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-372475, EBI-12811111;
CC P14678-2; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-372475, EBI-12805508;
CC P14678-2; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-372475, EBI-12111050;
CC P14678-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-372475, EBI-11962084;
CC P14678-2; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-372475, EBI-2686809;
CC P14678-2; Q9Y333: LSM2; NbExp=6; IntAct=EBI-372475, EBI-347416;
CC P14678-2; Q86UL8-2: MAGI2; NbExp=3; IntAct=EBI-372475, EBI-12081182;
CC P14678-2; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-372475, EBI-12516603;
CC P14678-2; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-372475, EBI-8487781;
CC P14678-2; P02795: MT2A; NbExp=3; IntAct=EBI-372475, EBI-996616;
CC P14678-2; O43482: OIP5; NbExp=3; IntAct=EBI-372475, EBI-536879;
CC P14678-2; A6NGQ2: OOEP; NbExp=3; IntAct=EBI-372475, EBI-18583589;
CC P14678-2; Q99471: PFDN5; NbExp=3; IntAct=EBI-372475, EBI-357275;
CC P14678-2; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-372475, EBI-373552;
CC P14678-2; Q8ND90: PNMA1; NbExp=6; IntAct=EBI-372475, EBI-302345;
CC P14678-2; P86480: PRR20D; NbExp=3; IntAct=EBI-372475, EBI-12754095;
CC P14678-2; P25788: PSMA3; NbExp=3; IntAct=EBI-372475, EBI-348380;
CC P14678-2; Q93062: RBPMS; NbExp=3; IntAct=EBI-372475, EBI-740322;
CC P14678-2; Q8HWS3: RFX6; NbExp=6; IntAct=EBI-372475, EBI-746118;
CC P14678-2; Q9UJW9: SERTAD3; NbExp=4; IntAct=EBI-372475, EBI-748621;
CC P14678-2; Q02447: SP3; NbExp=3; IntAct=EBI-372475, EBI-348158;
CC P14678-2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-372475, EBI-11959123;
CC P14678-2; O75177: SS18L1; NbExp=3; IntAct=EBI-372475, EBI-744674;
CC P14678-2; Q9UBB9: TFIP11; NbExp=6; IntAct=EBI-372475, EBI-1105213;
CC P14678-2; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-372475, EBI-17438286;
CC P14678-2; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-372475, EBI-3650647;
CC P14678-2; P36406: TRIM23; NbExp=3; IntAct=EBI-372475, EBI-740098;
CC P14678-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-372475, EBI-947187;
CC P14678-2; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-372475, EBI-11524408;
CC P14678-2; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-372475, EBI-11975223;
CC P14678-2; O00308: WWP2; NbExp=3; IntAct=EBI-372475, EBI-743923;
CC P14678-2; P52747: ZNF143; NbExp=3; IntAct=EBI-372475, EBI-2849334;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=SM-B';
CC IsoId=P14678-1; Sequence=Displayed;
CC Name=SM-B;
CC IsoId=P14678-2; Sequence=VSP_005914;
CC Name=SM-B1;
CC IsoId=P14678-3; Sequence=VSP_012221;
CC -!- PTM: Methylated by PRMT5 (By similarity). Arg-108 and Arg-112 are
CC dimethylated, probably to asymmetric dimethylarginine (PubMed:16087681,
CC Ref.10). {ECO:0000250|UniProtKB:P27048, ECO:0000269|PubMed:16087681,
CC ECO:0000269|Ref.10}.
CC -!- DISEASE: Cerebrocostomandibular syndrome (CCMS) [MIM:117650]: A
CC syndrome characterized by severe micrognathia, rib defects ranging from
CC a few dorsal rib segments to complete absence of ossification, and
CC intellectual disability. {ECO:0000269|PubMed:25047197,
CC ECO:0000269|PubMed:25504470}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Patients with the autoimmune disease systemic lupus
CC erythematosus (SLE) have autoantibodies directed against some of the
CC individual snRNP polypeptides. The most common autoantigen is called
CC Sm. B/b' bear Sm epitopes.
CC -!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD54488.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X17567; CAB57867.1; -; mRNA.
DR EMBL; X17568; CAB57868.1; -; mRNA.
DR EMBL; X15893; CAA33902.1; -; mRNA.
DR EMBL; AF134825; AAD54488.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF134822; AAD54488.1; JOINED; Genomic_DNA.
DR EMBL; AF134823; AAD54488.1; JOINED; Genomic_DNA.
DR EMBL; AF134824; AAD54488.1; JOINED; Genomic_DNA.
DR EMBL; AL049650; CAB46715.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10596.1; -; Genomic_DNA.
DR EMBL; CR456969; CAG33250.1; -; mRNA.
DR EMBL; AL049650; CAB46714.1; -; Genomic_DNA.
DR EMBL; M34081; AAA36578.1; -; mRNA.
DR EMBL; M34082; AAA36579.1; -; mRNA.
DR EMBL; X52979; CAA37170.1; -; Genomic_DNA.
DR EMBL; X52979; CAA37171.1; -; Genomic_DNA.
DR CCDS; CCDS13026.1; -. [P14678-1]
DR CCDS; CCDS13027.1; -. [P14678-2]
DR PIR; S09377; S09377.
DR RefSeq; NP_003082.1; NM_003091.3. [P14678-2]
DR RefSeq; NP_937859.1; NM_198216.1. [P14678-1]
DR PDB; 1D3B; X-ray; 2.00 A; B/D/F/H/J/L=1-91.
DR PDB; 3CW1; X-ray; 5.49 A; A/H/I/J=1-174.
DR PDB; 3JCR; EM; 7.00 A; O/o=1-240.
DR PDB; 3PGW; X-ray; 4.40 A; B/Q=1-229.
DR PDB; 4PJO; X-ray; 3.30 A; B/P/b/p=1-95.
DR PDB; 4WZJ; X-ray; 3.60 A; AA/AH/AO/BA/BH/BO/CA/CH/CO/DA/DH/DO=1-95.
DR PDB; 5MQF; EM; 5.90 A; f/m=1-240.
DR PDB; 5O9Z; EM; 4.50 A; X/f/m=1-240.
DR PDB; 5XJC; EM; 3.60 A; b/i=1-229.
DR PDB; 5YZG; EM; 4.10 A; b/i=1-229.
DR PDB; 5Z56; EM; 5.10 A; b/i=1-229.
DR PDB; 5Z57; EM; 6.50 A; b/i=1-229.
DR PDB; 5Z58; EM; 4.90 A; b/i=1-229.
DR PDB; 6AH0; EM; 5.70 A; U/f/i=1-229.
DR PDB; 6FF7; EM; 4.50 A; f/m=1-240.
DR PDB; 6ICZ; EM; 3.00 A; b/i=1-229.
DR PDB; 6ID0; EM; 2.90 A; b/i=1-229.
DR PDB; 6ID1; EM; 2.86 A; b/i=1-229.
DR PDB; 6QDV; EM; 3.30 A; b/k=6-87.
DR PDB; 6QW6; EM; 2.92 A; 4b/5b=1-240.
DR PDB; 6QX9; EM; 3.28 A; 1b/2b/4b/5b=1-240.
DR PDB; 6V4X; EM; 3.20 A; B=1-95.
DR PDB; 6Y53; EM; 7.10 A; m=1-240.
DR PDB; 6Y5Q; EM; 7.10 A; m=1-240.
DR PDB; 7A5P; EM; 5.00 A; b/m=1-240.
DR PDB; 7ABG; EM; 7.80 A; f/m=1-240.
DR PDB; 7ABI; EM; 8.00 A; f/m=1-240.
DR PDB; 7DVQ; EM; 2.89 A; b/i=1-240.
DR PDBsum; 1D3B; -.
DR PDBsum; 3CW1; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 3PGW; -.
DR PDBsum; 4PJO; -.
DR PDBsum; 4WZJ; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 5XJC; -.
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; 7DVQ; -.
DR AlphaFoldDB; P14678; -.
DR SMR; P14678; -.
DR BioGRID; 112512; 298.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-2392; U1 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-6033; Sm complex.
DR CORUM; P14678; -.
DR DIP; DIP-31239N; -.
DR IntAct; P14678; 148.
DR MINT; P14678; -.
DR STRING; 9606.ENSP00000412566; -.
DR iPTMnet; P14678; -.
DR MetOSite; P14678; -.
DR PhosphoSitePlus; P14678; -.
DR SwissPalm; P14678; -.
DR BioMuta; SNRPB; -.
DR DMDM; 134037; -.
DR EPD; P14678; -.
DR jPOST; P14678; -.
DR MassIVE; P14678; -.
DR MaxQB; P14678; -.
DR PaxDb; P14678; -.
DR PeptideAtlas; P14678; -.
DR PRIDE; P14678; -.
DR ProteomicsDB; 53074; -. [P14678-1]
DR ProteomicsDB; 53075; -. [P14678-2]
DR ProteomicsDB; 53076; -. [P14678-3]
DR TopDownProteomics; P14678-2; -. [P14678-2]
DR Antibodypedia; 4041; 158 antibodies from 27 providers.
DR DNASU; 6628; -.
DR Ensembl; ENST00000381342.7; ENSP00000370746.3; ENSG00000125835.20. [P14678-2]
DR Ensembl; ENST00000438552.6; ENSP00000412566.2; ENSG00000125835.20. [P14678-1]
DR GeneID; 6628; -.
DR KEGG; hsa:6628; -.
DR MANE-Select; ENST00000381342.7; ENSP00000370746.3; NM_003091.4; NP_003082.1. [P14678-2]
DR UCSC; uc002wfz.2; human. [P14678-1]
DR CTD; 6628; -.
DR DisGeNET; 6628; -.
DR GeneCards; SNRPB; -.
DR HGNC; HGNC:11153; SNRPB.
DR HPA; ENSG00000125835; Low tissue specificity.
DR MalaCards; SNRPB; -.
DR MIM; 117650; phenotype.
DR MIM; 182282; gene.
DR neXtProt; NX_P14678; -.
DR OpenTargets; ENSG00000125835; -.
DR Orphanet; 1393; Cerebrocostomandibular syndrome.
DR PharmGKB; PA35995; -.
DR VEuPathDB; HostDB:ENSG00000125835; -.
DR eggNOG; KOG3168; Eukaryota.
DR GeneTree; ENSGT00940000155052; -.
DR HOGENOM; CLU_076902_1_0_1; -.
DR OMA; KMINYRM; -.
DR OrthoDB; 1630470at2759; -.
DR PhylomeDB; P14678; -.
DR TreeFam; TF314232; -.
DR PathwayCommons; P14678; -.
DR Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; P14678; -.
DR BioGRID-ORCS; 6628; 761 hits in 1082 CRISPR screens.
DR ChiTaRS; SNRPB; human.
DR EvolutionaryTrace; P14678; -.
DR GeneWiki; SNRPB; -.
DR GenomeRNAi; 6628; -.
DR Pharos; P14678; Tbio.
DR PRO; PR:P14678; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P14678; protein.
DR Bgee; ENSG00000125835; Expressed in endometrium epithelium and 209 other tissues.
DR ExpressionAtlas; P14678; baseline and differential.
DR Genevisible; P14678; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IEA:Ensembl.
DR GO; GO:0034709; C:methylosome; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IPI:ComplexPortal.
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:0071004; C:U2-type prespliceosome; IBA:GO_Central.
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:0071208; F:histone pre-mRNA DCP binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IPI:BHF-UCL.
DR GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
DR GO; GO:1990446; F:U1 snRNP binding; IEA:Ensembl.
DR GO; GO:1990447; F:U2 snRNP binding; IEA:Ensembl.
DR GO; GO:0036261; P:7-methylguanosine cap hypermethylation; IC:ComplexPortal.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:MGI.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR IDEAL; IID00143; -.
DR InterPro; IPR001163; LSM_dom_euk/arc.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR017131; snRNP-assoc_SmB/SmN.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Disease variant; Intellectual disability; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW RNA-binding; Spliceosome.
FT CHAIN 1..240
FT /note="Small nuclear ribonucleoprotein-associated proteins
FT B and B'"
FT /id="PRO_0000125517"
FT REPEAT 175..181
FT REPEAT 191..196
FT REPEAT 216..221
FT REPEAT 222..228
FT REPEAT 230..236
FT REGION 163..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..236
FT /note="Repeat-rich region"
FT COMPBIAS 169..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 108
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 108
FT /note="Dimethylated arginine; in A2780 ovarian carcinoma
FT cell line"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 108
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 112
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 112
FT /note="Dimethylated arginine; in A2780 ovarian carcinoma
FT cell line"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 112
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 147
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|Ref.10"
FT MOD_RES 172
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P63162"
FT VAR_SEQ 227..228
FT /note="MR -> GCEAFFDPWPQSMEVAPQRRGLDSSGPRYHRPVCFLCCCSWSLMGL
FT SGFLT (in isoform SM-B1)"
FT /evidence="ECO:0000303|PubMed:2524838"
FT /id="VSP_012221"
FT VAR_SEQ 230..240
FT /note="PPPPGMRPPRP -> LL (in isoform SM-B)"
FT /evidence="ECO:0000303|PubMed:1694885,
FT ECO:0000303|PubMed:2522186, ECO:0000303|PubMed:2531083"
FT /id="VSP_005914"
FT VARIANT 55
FT /note="N -> S (in CCMS; expression of the protein is
FT reduced)"
FT /evidence="ECO:0000269|PubMed:25047197,
FT ECO:0000269|PubMed:25504470"
FT /id="VAR_073380"
FT VARIANT 55
FT /note="N -> T (in CCMS)"
FT /evidence="ECO:0000269|PubMed:25504470"
FT /id="VAR_073381"
FT VARIANT 56
FT /note="S -> R (in CCMS)"
FT /evidence="ECO:0000269|PubMed:25047197,
FT ECO:0000269|PubMed:25504470"
FT /id="VAR_073382"
FT VARIANT 56
FT /note="S -> W (in CCMS)"
FT /evidence="ECO:0000269|PubMed:25047197"
FT /id="VAR_073383"
FT VARIANT 79
FT /note="S -> P (in dbSNP:rs11545672)"
FT /id="VAR_052274"
FT CONFLICT 172..173
FT /note="RG -> L (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="Missing (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..218
FT /note="PP -> S (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1D3B"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1D3B"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:1D3B"
FT STRAND 40..51
FT /evidence="ECO:0007829|PDB:1D3B"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:4PJO"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:1D3B"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1D3B"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:1D3B"
SQ SEQUENCE 240 AA; 24610 MW; F2E1D5E11A601170 CRC64;
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK IKPKNSKQAE
REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA AGGPGIGRAA GRGIPAGVPM
PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV AAAAAAATAS IAGAPTQYPP GRGGPPPPMG
RGAPPPGMMG PPPGMRPPMG PPMGIPPGRG TPMGMPPPGM RPPPPGMRGP PPPGMRPPRP
