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P14678 - RSMB_HUMAN

UniProt

P14678 - RSMB_HUMAN

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Protein

Small nuclear ribonucleoprotein-associated proteins B and B'

Gene

SNRPB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 an 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.1 Publication

GO - Molecular functioni

  1. histone pre-mRNA DCP binding Source: Ensembl
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. histone mRNA metabolic process Source: Reactome
  3. mRNA 3'-end processing Source: Reactome
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. ncRNA metabolic process Source: Reactome
  6. RNA metabolic process Source: Reactome
  7. RNA splicing Source: Reactome
  8. spliceosomal snRNP assembly Source: UniProtKB
  9. termination of RNA polymerase II transcription Source: Reactome
  10. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Small nuclear ribonucleoprotein-associated proteins B and B'
Short name:
snRNP-B
Alternative name(s):
Sm protein B/B'
Short name:
Sm-B/B'
Short name:
SmB/B'
Gene namesi
Name:SNRPB
Synonyms:COD, SNRPB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:11153. SNRPB.

Subcellular locationi

Cytoplasm › cytosol 1 Publication. Nucleus 1 Publication
Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. histone pre-mRNA 3'end processing complex Source: Ensembl
  5. methylosome Source: UniProtKB
  6. nucleoplasm Source: Reactome
  7. small nuclear ribonucleoprotein complex Source: ProtInc
  8. SMN-Sm protein complex Source: UniProtKB
  9. spliceosomal complex Source: ProtInc
  10. U12-type spliceosomal complex Source: UniProtKB
  11. U1 snRNP Source: UniProtKB
  12. U4 snRNP Source: UniProtKB
  13. U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35995.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 240240Small nuclear ribonucleoprotein-associated proteins B and B'PRO_0000125517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei108 – 1081Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei112 – 1121Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei147 – 1471Omega-N-methylarginine1 Publication

Post-translational modificationi

Methylated. Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine.2 Publications

Keywords - PTMi

Methylation

Proteomic databases

MaxQBiP14678.
PaxDbiP14678.
PRIDEiP14678.

PTM databases

PhosphoSiteiP14678.

Expressioni

Gene expression databases

BgeeiP14678.
CleanExiHS_SNRPB.
ExpressionAtlasiP14678. baseline and differential.
GenevestigatoriP14678.

Organism-specific databases

HPAiCAB009610.
HPA003482.

Interactioni

Subunit structurei

U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an 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.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CLNS1AP541053EBI-372458,EBI-724693
SMN2Q16637-33EBI-372471,EBI-395447
SNRPD3P623182EBI-372458,EBI-372789

Protein-protein interaction databases

BioGridi112512. 96 interactions.
DIPiDIP-31239N.
IntActiP14678. 43 interactions.
MINTiMINT-124876.
STRINGi9606.ENSP00000412566.

Structurei

Secondary structure

1
240
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Beta strandi15 – 217Combined sources
Beta strandi26 – 338Combined sources
Beta strandi40 – 5112Combined sources
Beta strandi61 – 7212Combined sources
Helixi74 – 763Combined sources
Beta strandi77 – 848Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3BX-ray2.00B/D/F/H/J/L1-91[»]
3CW1X-ray5.49A/H/I/J1-174[»]
3PGWX-ray4.40B/Q1-229[»]
4V5UX-ray3.60A/H/O1-95[»]
ProteinModelPortaliP14678.
SMRiP14678. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14678.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati175 – 1817
Repeati191 – 1966
Repeati216 – 2216
Repeati222 – 2287
Repeati230 – 2367

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 23662Repeat-rich regionAdd
BLAST

Sequence similaritiesi

Belongs to the snRNP SmB/SmN family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00670000098029.
HOGENOMiHOG000188899.
HOVERGENiHBG001019.
KOiK11086.
OMAiSSGPRYH.
OrthoDBiEOG7J70HT.
PhylomeDBiP14678.
TreeFamiTF314232.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037187. snRNP_SmB/SmN. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform SM-B' (identifier: P14678-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK 
        60         70         80         90        100
IKPKNSKQAE REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA 
       110        120        130        140        150
AGGPGIGRAA GRGIPAGVPM PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV 
       160        170        180        190        200
AAAAAAATAS IAGAPTQYPP GRGGPPPPMG RGAPPPGMMG PPPGMRPPMG 
       210        220        230        240
PPMGIPPGRG TPMGMPPPGM RPPPPGMRGP PPPGMRPPRP
Length:240
Mass (Da):24,610
Last modified:November 1, 1991 - v2
Checksum:iF2E1D5E11A601170
GO
Isoform SM-B (identifier: P14678-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     230-240: PPPPGMRPPRP → LL

Show »
Length:231
Mass (Da):23,656
Checksum:i5CB0BB2E75B93D4A
GO
Isoform SM-B1 (identifier: P14678-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-228: MR → GCEAFFDPWPQSMEVAPQRRGLDSSGPRYHRPVCFLCCCSWSLMGLSGFLT

Show »
Length:289
Mass (Da):30,032
Checksum:i573E8A21414E2C22
GO

Sequence cautioni

The sequence AAD54488.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1732RG → L(PubMed:2524838)Curated
Sequence conflicti201 – 2011Missing(PubMed:2524838)Curated
Sequence conflicti217 – 2182PP → S(PubMed:2524838)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti79 – 791S → P.
Corresponds to variant rs11545672 [ dbSNP | Ensembl ].		VAR_052274

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei227 – 2282MR → GCEAFFDPWPQSMEVAPQRR GLDSSGPRYHRPVCFLCCCS WSLMGLSGFLT in isoform SM-B1. 1 PublicationVSP_012221
Alternative sequencei230 – 24011PPPPGMRPPRP → LL in isoform SM-B. 3 PublicationsVSP_005914Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17567 mRNA. Translation: CAB57867.1.
X17568 mRNA. Translation: CAB57868.1.
X15893 mRNA. Translation: CAA33902.1.
AF134825
, AF134822, AF134823, AF134824 Genomic DNA. Translation: AAD54488.1. Sequence problems.
AL049650 Genomic DNA. Translation: CAB46715.1.
CH471133 Genomic DNA. Translation: EAX10596.1.
CR456969 mRNA. Translation: CAG33250.1.
AL049650 Genomic DNA. Translation: CAB46714.1.
M34081 mRNA. Translation: AAA36578.1.
M34082 mRNA. Translation: AAA36579.1.
X52979 Genomic DNA. Translation: CAA37170.1.
X52979 Genomic DNA. Translation: CAA37171.1.
CCDSiCCDS13026.1. [P14678-1]
CCDS13027.1. [P14678-2]
PIRiS09377.
RefSeqiNP_003082.1. NM_003091.3. [P14678-2]
NP_937859.1. NM_198216.1. [P14678-1]
UniGeneiHs.83753.

Genome annotation databases

EnsembliENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2]
ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1]
GeneIDi6628.
KEGGihsa:6628.
UCSCiuc002wfz.1. human. [P14678-1]

Polymorphism databases

DMDMi134037.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17567 mRNA. Translation: CAB57867.1.
X17568 mRNA. Translation: CAB57868.1.
X15893 mRNA. Translation: CAA33902.1.
AF134825
, AF134822, AF134823, AF134824 Genomic DNA. Translation: AAD54488.1. Sequence problems.
AL049650 Genomic DNA. Translation: CAB46715.1.
CH471133 Genomic DNA. Translation: EAX10596.1.
CR456969 mRNA. Translation: CAG33250.1.
AL049650 Genomic DNA. Translation: CAB46714.1.
M34081 mRNA. Translation: AAA36578.1.
M34082 mRNA. Translation: AAA36579.1.
X52979 Genomic DNA. Translation: CAA37170.1.
X52979 Genomic DNA. Translation: CAA37171.1.
CCDSiCCDS13026.1. [P14678-1]
CCDS13027.1. [P14678-2]
PIRiS09377.
RefSeqiNP_003082.1. NM_003091.3. [P14678-2]
NP_937859.1. NM_198216.1. [P14678-1]
UniGeneiHs.83753.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D3BX-ray2.00B/D/F/H/J/L1-91[»]
3CW1X-ray5.49A/H/I/J1-174[»]
3PGWX-ray4.40B/Q1-229[»]
4V5UX-ray3.60A/H/O1-95[»]
ProteinModelPortaliP14678.
SMRiP14678. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112512. 96 interactions.
DIPiDIP-31239N.
IntActiP14678. 43 interactions.
MINTiMINT-124876.
STRINGi9606.ENSP00000412566.

PTM databases

PhosphoSiteiP14678.

Polymorphism databases

DMDMi134037.

Proteomic databases

MaxQBiP14678.
PaxDbiP14678.
PRIDEiP14678.

Protocols and materials databases

DNASUi6628.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381342; ENSP00000370746; ENSG00000125835. [P14678-2]
ENST00000438552; ENSP00000412566; ENSG00000125835. [P14678-1]
GeneIDi6628.
KEGGihsa:6628.
UCSCiuc002wfz.1. human. [P14678-1]

Organism-specific databases

CTDi6628.
GeneCardsiGC20M002442.
HGNCiHGNC:11153. SNRPB.
HPAiCAB009610.
HPA003482.
MIMi182282. gene.
neXtProtiNX_P14678.
PharmGKBiPA35995.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00670000098029.
HOGENOMiHOG000188899.
HOVERGENiHBG001019.
KOiK11086.
OMAiSSGPRYH.
OrthoDBiEOG7J70HT.
PhylomeDBiP14678.
TreeFamiTF314232.

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSNRPB. human.
EvolutionaryTraceiP14678.
GeneWikiiSNRPB.
GenomeRNAii6628.
NextBioi25817.
PROiP14678.
SOURCEiSearch...

Gene expression databases

BgeeiP14678.
CleanExiHS_SNRPB.
ExpressionAtlasiP14678. baseline and differential.
GenevestigatoriP14678.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
IPR017131. snRNP-assoc_SmB/SmN.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037187. snRNP_SmB/SmN. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloned human snRNP proteins B and B' differ only in their carboxy-terminal part."
    van Dam A., Winkel I., Zijlstra-Baalbergen J., Smeenk R., Cuypers H.T.
    EMBO J. 8:3853-3860(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SM-B AND SM-B').
  2. "A comparison of snRNP-associated Sm-autoantigens: human N, rat N and human B/B'."
    Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.
    Nucleic Acids Res. 17:1733-1743(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SM-B).
    Tissue: Thyroid carcinoma.
  3. Erratum
    Schmauss C., McAllister G., Ohosone Y., Hardin J.A., Lerner M.R.
    Nucleic Acids Res. 17:6777-6777(1989)
  4. "Molecular cloning of cDNA encoding Sm autoantigen: derivation of a cDNA for a B polypeptide of the U series of small nuclear ribonucleoprotein particles."
    Ohosone Y., Mimori T., Griffith A., Akizuki M., Homma M., Craft J., Hardin J.A.
    Proc. Natl. Acad. Sci. U.S.A. 86:4249-4253(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SM-B1).
    Tissue: Fibroblast.
  5. "Concerted regulation and molecular evolution of the duplicated SNRPB'/B and SNRPN loci."
    Gray T.A., Smithwick M.J., Schaldach M.A., Martone D.L., Graves J.A., McCarrey J.R., Nicholls R.D.
    Nucleic Acids Res. 27:4577-4584(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SM-B').
  7. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "Epitope mapping of recombinant HeLa SmB and B' peptides obtained by the polymerase chain reaction."
    Elkon K.B., Hines J.J., Chu J.-L., Parnassa A.
    J. Immunol. 145:636-643(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-240 (ISOFORMS SM-B AND SM-B').
  10. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 9-16; 19-32 AND 66-147, METHYLATION AT ARG-108; ARG-112 AND ARG-147, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  11. "The small nuclear ribonucleoproteins, SmB and B', are products of a single gene."
    Chu J.-L., Elkon K.B.
    Gene 97:311-312(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 209-240.
  12. "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein."
    Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.
    EMBO J. 20:5470-5479(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE U7 SNRNP COMPLEX.
  13. "SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta."
    Narayanan U., Ospina J.K., Frey M.R., Hebert M.D., Matera A.G.
    Hum. Mol. Genet. 11:1785-1795(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX20; SNUPN AND SMN1.
  14. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  15. "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."
    Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R., Fischer U., Schuemperli D.
    Genes Dev. 17:2321-2333(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LSM11.
    Tissue: Cervix carcinoma.
  16. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
    Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
    RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Tudor domains bind symmetrical dimethylated arginines."
    Cote J., Richard S.
    J. Biol. Chem. 280:28476-28483(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TDRD3.
  18. "Toward an assembly line for U7 snRNPs: interactions of U7-specific Lsm proteins with PRMT5 and SMN complexes."
    Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C., Fischer U., Schuemperli D.
    J. Biol. Chem. 280:34435-34440(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLNS1A AND SMN, METHYLATION.
  19. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
    Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
    Cell 135:497-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX, SUBCELLULAR LOCATION.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs."
    Kambach C., Walke S., Young R., Avis J.M., de la Fortelle E., Raker V.A., Luehrmann R., Li J., Nagai K.
    Cell 96:375-387(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  22. "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
    Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
    Nature 458:475-480(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-174 IN SPLICEOSOMAL U1 SNRNP.
  23. "Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis."
    Leung A.K., Nagai K., Li J.
    Nature 473:536-539(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-95 IN SPLICEOSOMAL CORE U4 SNRNP.
+Additional computationally mapped references.

Entry informationi

Entry nameiRSMB_HUMAN
AccessioniPrimary (citable) accession number: P14678
Secondary accession number(s): Q15490, Q6IB35, Q9UIS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1991
Last modified: February 4, 2015
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.