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P14678

- RSMB_HUMAN

UniProt

P14678 - RSMB_HUMAN

Protein

Small nuclear ribonucleoprotein-associated proteins B and B'

Gene

SNRPB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    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
    3. protein binding Source: IntAct

    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

    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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11153. SNRPB.

    Subcellular locationi

    Cytoplasmcytosol 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: UniProt
    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

    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 – 1081Omega-N-methylated arginine2 Publications
    Modified residuei112 – 1121Dimethylated arginine; in A2780 ovarian carcinoma cell line2 Publications
    Modified residuei112 – 1121Omega-N-methylated arginine2 Publications
    Modified residuei147 – 1471Omega-N-methylarginine2 Publications

    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

    ArrayExpressiP14678.
    BgeeiP14678.
    CleanExiHS_SNRPB.
    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. 81 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 – 123
    Beta strandi15 – 217
    Beta strandi26 – 338
    Beta strandi40 – 5112
    Beta strandi61 – 7212
    Helixi74 – 763
    Beta strandi77 – 848

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1D3BX-ray2.00B/D/F/H/J/L1-91[»]
    2Y9AX-ray3.60A/H/O1-95[»]
    2Y9BX-ray3.60A/H/O1-95[»]
    2Y9CX-ray3.60A/H/O1-95[»]
    2Y9DX-ray3.60A/H/O1-95[»]
    3CW1X-ray5.49A/H/I/J1-174[»]
    3PGWX-ray4.40B/Q1-229[»]
    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.
    HOGENOMiHOG000188899.
    HOVERGENiHBG001019.
    KOiK11086.
    OMAiKNNKMIQ.
    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

    MTVGKSSKML QHIDYRMRCI LQDGRIFIGT FKAFDKHMNL ILCDCDEFRK    50
    IKPKNSKQAE REEKRVLGLV LLRGENLVSM TVEGPPPKDT GIARVPLAGA 100
    AGGPGIGRAA GRGIPAGVPM PQAPAGLAGP VRGVGGPSQQ VMTPQGRGTV 150
    AAAAAAATAS IAGAPTQYPP GRGGPPPPMG RGAPPPGMMG PPPGMRPPMG 200
    PPMGIPPGRG TPMGMPPPGM RPPPPGMRGP PPPGMRPPRP 240
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13026.1. [P14678-1 ]
    CCDS13027.1. [P14678-2 ]
    PIRi S09377.
    RefSeqi NP_003082.1. NM_003091.3. [P14678-2 ]
    NP_937859.1. NM_198216.1. [P14678-1 ]
    UniGenei Hs.83753.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1D3B X-ray 2.00 B/D/F/H/J/L 1-91 [» ]
    2Y9A X-ray 3.60 A/H/O 1-95 [» ]
    2Y9B X-ray 3.60 A/H/O 1-95 [» ]
    2Y9C X-ray 3.60 A/H/O 1-95 [» ]
    2Y9D X-ray 3.60 A/H/O 1-95 [» ]
    3CW1 X-ray 5.49 A/H/I/J 1-174 [» ]
    3PGW X-ray 4.40 B/Q 1-229 [» ]
    ProteinModelPortali P14678.
    SMRi P14678. Positions 1-95.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112512. 81 interactions.
    DIPi DIP-31239N.
    IntActi P14678. 43 interactions.
    MINTi MINT-124876.
    STRINGi 9606.ENSP00000412566.

    PTM databases

    PhosphoSitei P14678.

    Polymorphism databases

    DMDMi 134037.

    Proteomic databases

    MaxQBi P14678.
    PaxDbi P14678.
    PRIDEi P14678.

    Protocols and materials databases

    DNASUi 6628.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381342 ; ENSP00000370746 ; ENSG00000125835 . [P14678-2 ]
    ENST00000438552 ; ENSP00000412566 ; ENSG00000125835 . [P14678-1 ]
    GeneIDi 6628.
    KEGGi hsa:6628.
    UCSCi uc002wfz.1. human. [P14678-1 ]

    Organism-specific databases

    CTDi 6628.
    GeneCardsi GC20M002442.
    HGNCi HGNC:11153. SNRPB.
    HPAi CAB009610.
    HPA003482.
    MIMi 182282. gene.
    neXtProti NX_P14678.
    PharmGKBi PA35995.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1958.
    HOGENOMi HOG000188899.
    HOVERGENi HBG001019.
    KOi K11086.
    OMAi KNNKMIQ.
    OrthoDBi EOG7J70HT.
    PhylomeDBi P14678.
    TreeFami TF314232.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi SNRPB. human.
    EvolutionaryTracei P14678.
    GeneWikii SNRPB.
    GenomeRNAii 6628.
    NextBioi 25817.
    PROi P14678.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14678.
    Bgeei P14678.
    CleanExi HS_SNRPB.
    Genevestigatori P14678.

    Family and domain databases

    InterProi IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    IPR017131. snRNP-assoc_SmB/SmN.
    [Graphical view ]
    Pfami PF01423. LSM. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037187. snRNP_SmB/SmN. 1 hit.
    SMARTi SM00651. Sm. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50182. SSF50182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    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: October 1, 2014
    This is version 169 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