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Small nuclear ribonucleoprotein-associated proteins B and B' (snRNP-B) (Sm protein B/B') (Sm-B/B') (SmB/B')

 RSMB_HUMAN              Reviewed;         240 AA.
P14678; Q15490; Q6IB35; Q9UIS5;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 2.
30-AUG-2017, entry version 199.
RecName: Full=Small nuclear ribonucleoprotein-associated proteins B and B';
Short=snRNP-B;
AltName: Full=Sm protein B/B';
Short=Sm-B/B';
Short=SmB/B';
Name=SNRPB; Synonyms=COD, SNRPB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SM-B AND SM-B').
PubMed=2531083;
van Dam A., Winkel I., Zijlstra-Baalbergen J., Smeenk R.,
Cuypers H.T.;
"Cloned human snRNP proteins B and B' differ only in their carboxy-
terminal part.";
EMBO J. 8:3853-3860(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SM-B).
TISSUE=Thyroid carcinoma;
PubMed=2522186; DOI=10.1093/nar/17.4.1733;
Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.;
"A comparison of snRNP-associated Sm-autoantigens: human N, rat N and
human B/B'.";
Nucleic Acids Res. 17:1733-1743(1989).
[3]
ERRATUM.
Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.;
Nucleic Acids Res. 17:6777-6777(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SM-B1).
TISSUE=Fibroblast;
PubMed=2524838; DOI=10.1073/pnas.86.11.4249;
Ohosone Y., Mimori T., Griffith A., Akizuki M., Homma M., Craft J.,
Hardin J.A.;
"Molecular cloning of cDNA encoding Sm autoantigen: derivation of a
cDNA for a B polypeptide of the U series of small nuclear
ribonucleoprotein particles.";
Proc. Natl. Acad. Sci. U.S.A. 86:4249-4253(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10556313; DOI=10.1093/nar/27.23.4577;
Gray T.A., Smithwick M.J., Schaldach M.A., Martone D.L., Graves J.A.,
McCarrey J.R., Nicholls R.D.;
"Concerted regulation and molecular evolution of the duplicated
SNRPB'/B and SNRPN loci.";
Nucleic Acids Res. 27:4577-4584(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SM-B').
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-240 (ISOFORMS SM-B AND SM-B').
PubMed=1694885;
Elkon K.B., Hines J.J., Chu J.-L., Parnassa A.;
"Epitope mapping of recombinant HeLa SmB and B' peptides obtained by
the polymerase chain reaction.";
J. Immunol. 145:636-643(1990).
[10]
PROTEIN SEQUENCE OF 9-16; 19-32 AND 66-147, METHYLATION AT ARG-108;
ARG-112 AND ARG-147, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 209-240.
PubMed=1825643; DOI=10.1016/0378-1119(91)90069-N;
Chu J.-L., Elkon K.B.;
"The small nuclear ribonucleoproteins, SmB and B', are products of a
single gene.";
Gene 97:311-312(1991).
[12]
IDENTIFICATION IN THE U7 SNRNP COMPLEX.
PubMed=11574479; DOI=10.1093/emboj/20.19.5470;
Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.;
"Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10,
a new 14 kDa Sm D1-like protein.";
EMBO J. 20:5470-5479(2001).
[13]
INTERACTION WITH DDX20; SNUPN AND SMN1.
PubMed=12095920; DOI=10.1093/hmg/11.15.1785;
Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.;
"SMN, the spinal muscular atrophy protein, forms a pre-import snRNP
complex with snurportin1 and importin beta.";
Hum. Mol. Genet. 11:1785-1795(2002).
[14]
IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[15]
INTERACTION WITH LSM11.
TISSUE=Cervix carcinoma;
PubMed=12975319; DOI=10.1101/gad.274403;
Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R.,
Fischer U., Schuemperli D.;
"Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN
complex and the role of a new component, Lsm11, in histone RNA
processing.";
Genes Dev. 17:2321-2333(2003).
[16]
IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15146077; DOI=10.1261/rna.7320604;
Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R.,
Elbashir S., Tuschl T., Luehrmann R.;
"The human 18S U11/U12 snRNP contains a set of novel proteins not
found in the U2-dependent spliceosome.";
RNA 10:929-941(2004).
[17]
INTERACTION WITH TDRD3.
PubMed=15955813; DOI=10.1074/jbc.M414328200;
Cote J., Richard S.;
"Tudor domains bind symmetrical dimethylated arginines.";
J. Biol. Chem. 280:28476-28483(2005).
[18]
INTERACTION WITH CLNS1A AND SMN, AND METHYLATION.
PubMed=16087681; DOI=10.1074/jbc.M505077200;
Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
Fischer U., Schuemperli D.;
"Toward an assembly line for U7 snRNPs: interactions of U7-specific
Lsm proteins with PRMT5 and SMN complexes.";
J. Biol. Chem. 280:34435-34440(2005).
[19]
FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX,
IDENTIFICATION IN SMN-SM COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
Englbrecht C., Sickmann A., Stark H., Fischer U.;
"An assembly chaperone collaborates with the SMN complex to generate
spliceosomal SnRNPs.";
Cell 135:497-509(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-108 AND ARG-112, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[22]
INVOLVEMENT IN CCMS, VARIANTS CCMS SER-55; ARG-56 AND TRP-56, AND
CHARACTERIZATION OF VARIANTS CCMS SER-55.
PubMed=25047197; DOI=10.1038/ncomms5483;
Care4Rare Canada;
Lynch D.C., Revil T., Schwartzentruber J., Bhoj E.J., Innes A.M.,
Lamont R.E., Lemire E.G., Chodirker B.N., Taylor J.P., Zackai E.H.,
McLeod D.R., Kirk E.P., Hoover-Fong J., Fleming L., Savarirayan R.,
Majewski J., Jerome-Majewska L.A., Parboosingh J.S., Bernier F.P.;
"Disrupted auto-regulation of the spliceosomal gene SNRPB causes
cerebro-costo-mandibular syndrome.";
Nat. Commun. 5:4483-4483(2014).
[23]
INVOLVEMENT IN CCMS, AND VARIANTS CCMS SER-55; THR-55 AND ARG-56.
PubMed=25504470; DOI=10.1002/humu.22729;
Bacrot S., Doyard M., Huber C., Alibeu O., Feldhahn N., Lehalle D.,
Lacombe D., Marlin S., Nitschke P., Petit F., Vazquez M.P.,
Munnich A., Cormier-Daire V.;
"Mutations in SNRPB, encoding components of the core splicing
machinery, cause cerebro-costo-mandibular syndrome.";
Hum. Mutat. 36:187-190(2015).
[24]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=10025403; DOI=10.1016/S0092-8674(00)80550-4;
Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E.,
Raker V.A., Luehrmann R., Li J., Nagai K.;
"Crystal structures of two Sm protein complexes and their implications
for the assembly of the spliceosomal snRNPs.";
Cell 96:375-387(1999).
[25]
X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-174 IN SPLICEOSOMAL U1
SNRNP.
PubMed=19325628; DOI=10.1038/nature07851;
Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.;
"Crystal structure of human spliceosomal U1 snRNP at 5.5 A
resolution.";
Nature 458:475-480(2009).
[26]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-95 IN SPLICEOSOMAL CORE U4
SNRNP.
PubMed=21516107; DOI=10.1038/nature09956;
Leung A.K., Nagai K., Li J.;
"Structure of the spliceosomal U4 snRNP core domain and its
implication for snRNP biogenesis.";
Nature 473:536-539(2011).
-!- FUNCTION: Core component of the spliceosomal U1, U2, U4 and U5
small nuclear ribonucleoproteins (snRNPs), the building blocks of
the spliceosome. Thereby, plays an important role in the splicing
of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common
set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and
SNRPG that assemble in a heptameric protein ring on the Sm site of
the small nuclear RNA to form the core snRNP. As part of the U7
snRNP it is involved in histone 3'-end processing.
{ECO:0000269|PubMed:18984161}.
-!- SUBUNIT: U1 snRNP is for instance composed of the 7 core Sm
proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG
that assemble in a heptameric protein ring on the Sm site of the
small nuclear RNA to form the core snRNP, and at least three U1
snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C.
Component of the U11/U12 snRNPs that are part of the U12-type
spliceosome. Component of the heptameric ring U7 snRNP complex, or
U7 Sm protein core complex, at least composed of LSM10, LSM11,
SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Part of the SMN-
Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4,
GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins
SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes
core snRNPs assembly. Forms a 6S pICln-Sm complex composed of
CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like
structure where CLNS1A/pICln mimics additional Sm proteins and
which is unable to assemble into the core snRNP. Identified in a
histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP,
SNRPB, SYNCRIP and YBX1. Interacts with TDRD3 and SNUPN.
{ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12095920, ECO:0000269|PubMed:12975319,
ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:15955813,
ECO:0000269|PubMed:16087681, ECO:0000269|PubMed:18984161}.
-!- INTERACTION:
Q8N9N5:BANP; NbExp=3; IntAct=EBI-372475, EBI-744695;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-372475, EBI-739580;
O95400:CD2BP2; NbExp=5; IntAct=EBI-372475, EBI-768015;
Q53EZ4:CEP55; NbExp=3; IntAct=EBI-372475, EBI-747776;
P54105:CLNS1A; NbExp=4; IntAct=EBI-372475, EBI-724693;
Q9Y2V7:COG6; NbExp=4; IntAct=EBI-372475, EBI-3866319;
O75553:DAB1; NbExp=3; IntAct=EBI-372475, EBI-7875264;
P59022:DSCR10; NbExp=4; IntAct=EBI-372475, EBI-12127500;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-372475, EBI-618309;
Q6A162:KRT40; NbExp=3; IntAct=EBI-372475, EBI-10171697;
Q96JM7:L3MBTL3; NbExp=3; IntAct=EBI-372475, EBI-2686809;
Q8ND90:PNMA1; NbExp=5; IntAct=EBI-372475, EBI-302345;
P86480:PRR20D; NbExp=4; IntAct=EBI-372475, EBI-12754095;
P25788:PSMA3; NbExp=3; IntAct=EBI-372475, EBI-348380;
Q93062:RBPMS; NbExp=3; IntAct=EBI-372475, EBI-740322;
Q8HWS3:RFX6; NbExp=5; IntAct=EBI-372475, EBI-746118;
Q16637-3:SMN2; NbExp=3; IntAct=EBI-372471, EBI-395447;
P62318:SNRPD3; NbExp=2; IntAct=EBI-372458, EBI-372789;
O75177:SS18L1; NbExp=3; IntAct=EBI-372475, EBI-744674;
Q9UBB9:TFIP11; NbExp=5; IntAct=EBI-372475, EBI-1105213;
P36406:TRIM23; NbExp=3; IntAct=EBI-372475, EBI-740098;
Q9UHD9:UBQLN2; NbExp=4; IntAct=EBI-372475, EBI-947187;
O00308:WWP2; NbExp=4; IntAct=EBI-372475, EBI-743923;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:18984161}. Nucleus
{ECO:0000269|PubMed:18984161}. Note=SMN-mediated assembly into
core snRNPs occurs in the cytosol before SMN-mediated transport to
the nucleus to be included in spliceosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=SM-B';
IsoId=P14678-1; Sequence=Displayed;
Name=SM-B;
IsoId=P14678-2; Sequence=VSP_005914;
Name=SM-B1;
IsoId=P14678-3; Sequence=VSP_012221;
-!- PTM: Methylated. Arg-108 and Arg-112 are dimethylated, probably to
asymmetric dimethylarginine. {ECO:0000269|PubMed:16087681,
ECO:0000269|Ref.10}.
-!- DISEASE: Cerebrocostomandibular syndrome (CCMS) [MIM:117650]: A
syndrome characterized by severe micrognathia, rib defects ranging
from a few dorsal rib segments to complete absence of
ossification, and mental retardation.
{ECO:0000269|PubMed:25047197, ECO:0000269|PubMed:25504470}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Patients with the autoimmune disease systemic lupus
erythematosus (SLE) have autoantibodies directed against some of
the individual snRNP polypeptides. The most common autoantigen is
called Sm. B/b' bear Sm epitopes.
-!- SIMILARITY: Belongs to the snRNP SmB/SmN family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD54488.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X17567; CAB57867.1; -; mRNA.
EMBL; X17568; CAB57868.1; -; mRNA.
EMBL; X15893; CAA33902.1; -; mRNA.
EMBL; AF134825; AAD54488.1; ALT_SEQ; Genomic_DNA.
EMBL; AF134822; AAD54488.1; JOINED; Genomic_DNA.
EMBL; AF134823; AAD54488.1; JOINED; Genomic_DNA.
EMBL; AF134824; AAD54488.1; JOINED; Genomic_DNA.
EMBL; AL049650; CAB46715.1; -; Genomic_DNA.
EMBL; CH471133; EAX10596.1; -; Genomic_DNA.
EMBL; CR456969; CAG33250.1; -; mRNA.
EMBL; AL049650; CAB46714.1; -; Genomic_DNA.
EMBL; M34081; AAA36578.1; -; mRNA.
EMBL; M34082; AAA36579.1; -; mRNA.
EMBL; X52979; CAA37170.1; -; Genomic_DNA.
EMBL; X52979; CAA37171.1; -; Genomic_DNA.
CCDS; CCDS13026.1; -. [P14678-1]
CCDS; CCDS13027.1; -. [P14678-2]
PIR; S09377; S09377.
RefSeq; NP_003082.1; NM_003091.3. [P14678-2]
RefSeq; NP_937859.1; NM_198216.1. [P14678-1]
UniGene; Hs.83753; -.
PDB; 1D3B; X-ray; 2.00 A; B/D/F/H/J/L=1-91.
PDB; 3CW1; X-ray; 5.49 A; A/H/I/J=1-174.
PDB; 3JCR; EM; 7.00 A; O/o=1-240.
PDB; 3PGW; X-ray; 4.40 A; B/Q=1-229.
PDB; 4PJO; X-ray; 3.30 A; B/P/b/p=1-95.
PDB; 4WZJ; X-ray; 3.60 A; AA/AH/AO/BA/BH/BO/CA/CH/CO/DA/DH/DO=1-95.
PDB; 5MQF; EM; 5.90 A; f/m=1-240.
PDBsum; 1D3B; -.
PDBsum; 3CW1; -.
PDBsum; 3JCR; -.
PDBsum; 3PGW; -.
PDBsum; 4PJO; -.
PDBsum; 4WZJ; -.
PDBsum; 5MQF; -.
ProteinModelPortal; P14678; -.
SMR; P14678; -.
BioGrid; 112512; 152.
DIP; DIP-31239N; -.
IntAct; P14678; 99.
MINT; MINT-124876; -.
STRING; 9606.ENSP00000412566; -.
iPTMnet; P14678; -.
PhosphoSitePlus; P14678; -.
SwissPalm; P14678; -.
BioMuta; SNRPB; -.
DMDM; 134037; -.
EPD; P14678; -.
MaxQB; P14678; -.
PaxDb; P14678; -.
PeptideAtlas; P14678; -.
PRIDE; P14678; -.
TopDownProteomics; P14678-2; -. [P14678-2]
DNASU; 6628; -.
Ensembl; ENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2]
Ensembl; ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1]
GeneID; 6628; -.
KEGG; hsa:6628; -.
UCSC; uc002wfz.2; human. [P14678-1]
CTD; 6628; -.
DisGeNET; 6628; -.
GeneCards; SNRPB; -.
HGNC; HGNC:11153; SNRPB.
HPA; CAB009610; -.
HPA; HPA003482; -.
HPA; HPA067842; -.
MalaCards; SNRPB; -.
MIM; 117650; phenotype.
MIM; 182282; gene.
neXtProt; NX_P14678; -.
OpenTargets; ENSG00000125835; -.
Orphanet; 1393; Cerebro-costo-mandibular syndrome.
PharmGKB; PA35995; -.
eggNOG; KOG3168; Eukaryota.
eggNOG; COG1958; LUCA.
GeneTree; ENSGT00670000098029; -.
HOGENOM; HOG000188899; -.
HOVERGEN; HBG001019; -.
KO; K11086; -.
OMA; RGMGMMP; -.
PhylomeDB; P14678; -.
TreeFam; TF314232; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-111367; SLBP independent Processing of Histone Pre-mRNAs.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
Reactome; R-HSA-77588; SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
ChiTaRS; SNRPB; human.
EvolutionaryTrace; P14678; -.
GeneWiki; SNRPB; -.
GenomeRNAi; 6628; -.
PRO; PR:P14678; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000125835; -.
CleanEx; HS_SNRPB; -.
ExpressionAtlas; P14678; baseline and differential.
Genevisible; P14678; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IEA:Ensembl.
GO; GO:0034709; C:methylosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:ProtInc.
GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; TAS:ProtInc.
GO; GO:0005685; C:U1 snRNP; IDA:UniProtKB.
GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
GO; GO:0005687; C:U4 snRNP; IDA:UniProtKB.
GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IBA:GO_Central.
GO; GO:0005682; C:U5 snRNP; IBA:GO_Central.
GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
GO; GO:0071208; F:histone pre-mRNA DCP binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0070034; F:telomerase RNA binding; IPI:BHF-UCL.
GO; GO:0030620; F:U2 snRNA binding; IPI:BHF-UCL.
GO; GO:0008334; P:histone mRNA metabolic process; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0051170; P:nuclear import; TAS:Reactome.
GO; GO:0006479; P:protein methylation; IDA:MGI.
GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
InterPro; IPR010920; LSM_dom.
InterPro; IPR001163; LSM_dom_euk/arc.
InterPro; IPR017131; snRNP-assoc_SmB/SmN.
Pfam; PF01423; LSM; 1.
PIRSF; PIRSF037187; snRNP_SmB/SmN; 1.
SMART; SM00651; Sm; 1.
SUPFAM; SSF50182; SSF50182; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Mental retardation;
Methylation; mRNA processing; mRNA splicing; Nucleus; Polymorphism;
Reference proteome; Repeat; Ribonucleoprotein; RNA-binding;
Spliceosome.
CHAIN 1 240 Small nuclear ribonucleoprotein-
associated proteins B and B'.
/FTId=PRO_0000125517.
REPEAT 175 181
REPEAT 191 196
REPEAT 216 221
REPEAT 222 228
REPEAT 230 236
REGION 175 236 Repeat-rich region.
MOD_RES 108 108 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 108 108 Dimethylated arginine; in A2780 ovarian
carcinoma cell line.
{ECO:0000269|Ref.10}.
MOD_RES 108 108 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 112 112 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 112 112 Dimethylated arginine; in A2780 ovarian
carcinoma cell line.
{ECO:0000269|Ref.10}.
MOD_RES 112 112 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 147 147 Omega-N-methylarginine.
{ECO:0000269|Ref.10}.
MOD_RES 172 172 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P63162}.
VAR_SEQ 227 228 MR -> GCEAFFDPWPQSMEVAPQRRGLDSSGPRYHRPVCF
LCCCSWSLMGLSGFLT (in isoform SM-B1).
{ECO:0000303|PubMed:2524838}.
/FTId=VSP_012221.
VAR_SEQ 230 240 PPPPGMRPPRP -> LL (in isoform SM-B).
{ECO:0000303|PubMed:1694885,
ECO:0000303|PubMed:2522186,
ECO:0000303|PubMed:2531083}.
/FTId=VSP_005914.
VARIANT 55 55 N -> S (in CCMS; expression of the
protein is reduced).
{ECO:0000269|PubMed:25047197,
ECO:0000269|PubMed:25504470}.
/FTId=VAR_073380.
VARIANT 55 55 N -> T (in CCMS).
{ECO:0000269|PubMed:25504470}.
/FTId=VAR_073381.
VARIANT 56 56 S -> R (in CCMS).
{ECO:0000269|PubMed:25047197,
ECO:0000269|PubMed:25504470}.
/FTId=VAR_073382.
VARIANT 56 56 S -> W (in CCMS).
{ECO:0000269|PubMed:25047197}.
/FTId=VAR_073383.
VARIANT 79 79 S -> P (in dbSNP:rs11545672).
/FTId=VAR_052274.
CONFLICT 172 173 RG -> L (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 201 201 Missing (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 217 218 PP -> S (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
HELIX 10 12 {ECO:0000244|PDB:1D3B}.
STRAND 15 21 {ECO:0000244|PDB:1D3B}.
STRAND 26 33 {ECO:0000244|PDB:1D3B}.
STRAND 40 51 {ECO:0000244|PDB:1D3B}.
STRAND 54 58 {ECO:0000244|PDB:4PJO}.
STRAND 61 72 {ECO:0000244|PDB:1D3B}.
HELIX 74 76 {ECO:0000244|PDB:1D3B}.
STRAND 77 84 {ECO:0000244|PDB:1D3B}.
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


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