Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P62310

- LSM3_HUMAN

UniProt

P62310 - LSM3_HUMAN

Protein

U6 snRNA-associated Sm-like protein LSm3

Gene

LSM3

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

    Binds specifically to the 3'-terminal U-tract of U6 snRNA.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. mRNA processing Source: UniProtKB
    5. mRNA splicing, via spliceosome Source: UniProtKB
    6. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    7. RNA metabolic process Source: Reactome

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U6 snRNA-associated Sm-like protein LSm3
    Gene namesi
    Name:LSM3
    ORF Names:MDS017
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:17874. LSM3.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134881991.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 102101U6 snRNA-associated Sm-like protein LSm3PRO_0000125560Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62310.
    PaxDbiP62310.
    PeptideAtlasiP62310.
    PRIDEiP62310.

    PTM databases

    PhosphoSiteiP62310.

    Expressioni

    Gene expression databases

    BgeeiP62310.
    CleanExiHS_LSM3.
    GenevestigatoriP62310.

    Organism-specific databases

    HPAiHPA044966.

    Interactioni

    Subunit structurei

    LSm subunits form a heteromer with a doughnut shape. Identified in the spliceosome C complex.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM1O151163EBI-348239,EBI-347619
    LSM10Q969L44EBI-348239,EBI-373268
    LSM2Q9Y33311EBI-348239,EBI-347416
    LSM5Q9Y4Y93EBI-348239,EBI-373007
    LSM6P623123EBI-348239,EBI-373310
    LSM7Q9UK454EBI-348239,EBI-348372
    LSM8O957776EBI-348239,EBI-347779
    YBX1P678092EBI-348239,EBI-354065

    Protein-protein interaction databases

    BioGridi118105. 32 interactions.
    DIPiDIP-31218N.
    IntActiP62310. 26 interactions.
    MINTiMINT-1036960.
    STRINGi9606.ENSP00000302160.

    Structurei

    3D structure databases

    ProteinModelPortaliP62310.
    SMRiP62310. Positions 16-98.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the snRNP Sm proteins family.Curated

    Phylogenomic databases

    eggNOGiNOG236203.
    HOGENOMiHOG000223550.
    HOVERGENiHBG052368.
    InParanoidiP62310.
    KOiK12622.
    OMAiGYDSHCN.
    OrthoDBiEOG76HQ4Q.
    PhylomeDBiP62310.
    TreeFamiTF312907.

    Family and domain databases

    InterProiIPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view]
    PfamiPF01423. LSM. 1 hit.
    [Graphical view]
    SMARTiSM00651. Sm. 1 hit.
    [Graphical view]
    SUPFAMiSSF50182. SSF50182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P62310-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADDVDQQQT TNTVEEPLDL IRLSLDERIY VKMRNDRELR GRLHAYDQHL    50
    NMILGDVEET VTTIEIDEET YEEIYKSTKR NIPMLFVRGD GVVLVAPPLR 100
    VG 102
    Length:102
    Mass (Da):11,845
    Last modified:January 23, 2007 - v2
    Checksum:i206B0DF0D95CD4D2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238095 mRNA. Translation: CAB45866.1.
    AF182289 mRNA. Translation: AAD56227.1.
    AF182418 mRNA. Translation: AAG14954.1.
    CR457185 mRNA. Translation: CAG33466.1.
    CH471055 Genomic DNA. Translation: EAW64190.1.
    BC007055 mRNA. Translation: AAH07055.1.
    CCDSiCCDS2619.1.
    RefSeqiNP_055278.1. NM_014463.2.
    UniGeneiHs.111632.

    Genome annotation databases

    EnsembliENST00000306024; ENSP00000302160; ENSG00000170860.
    GeneIDi27258.
    KEGGihsa:27258.
    UCSCiuc003byn.3. human.

    Polymorphism databases

    DMDMi61227725.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238095 mRNA. Translation: CAB45866.1 .
    AF182289 mRNA. Translation: AAD56227.1 .
    AF182418 mRNA. Translation: AAG14954.1 .
    CR457185 mRNA. Translation: CAG33466.1 .
    CH471055 Genomic DNA. Translation: EAW64190.1 .
    BC007055 mRNA. Translation: AAH07055.1 .
    CCDSi CCDS2619.1.
    RefSeqi NP_055278.1. NM_014463.2.
    UniGenei Hs.111632.

    3D structure databases

    ProteinModelPortali P62310.
    SMRi P62310. Positions 16-98.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118105. 32 interactions.
    DIPi DIP-31218N.
    IntActi P62310. 26 interactions.
    MINTi MINT-1036960.
    STRINGi 9606.ENSP00000302160.

    PTM databases

    PhosphoSitei P62310.

    Polymorphism databases

    DMDMi 61227725.

    Proteomic databases

    MaxQBi P62310.
    PaxDbi P62310.
    PeptideAtlasi P62310.
    PRIDEi P62310.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000306024 ; ENSP00000302160 ; ENSG00000170860 .
    GeneIDi 27258.
    KEGGi hsa:27258.
    UCSCi uc003byn.3. human.

    Organism-specific databases

    CTDi 27258.
    GeneCardsi GC03P014219.
    HGNCi HGNC:17874. LSM3.
    HPAi HPA044966.
    MIMi 607283. gene.
    neXtProti NX_P62310.
    PharmGKBi PA134881991.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236203.
    HOGENOMi HOG000223550.
    HOVERGENi HBG052368.
    InParanoidi P62310.
    KOi K12622.
    OMAi GYDSHCN.
    OrthoDBi EOG76HQ4Q.
    PhylomeDBi P62310.
    TreeFami TF312907.

    Enzyme and pathway databases

    Reactomei REACT_20518. mRNA decay by 5' to 3' exoribonuclease.

    Miscellaneous databases

    ChiTaRSi LSM3. human.
    GeneWikii LSM3.
    GenomeRNAii 27258.
    NextBioi 50206.
    PROi P62310.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62310.
    CleanExi HS_LSM3.
    Genevestigatori P62310.

    Family and domain databases

    InterProi IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view ]
    Pfami PF01423. LSM. 1 hit.
    [Graphical view ]
    SMARTi SM00651. Sm. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50182. SSF50182. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin."
      Salgado-Garrido J., Bragado-Nilsson E., Kandels-Lewis S., Seraphin B.
      EMBO J. 18:3451-3462(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal liver and Spleen.
    2. "A doughnut-shaped heteromer of human Sm-like proteins binds to the 3'-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro."
      Achsel T., Brahms H., Kastner B., Bachi A., Wilm M., Luehrmann R.
      EMBO J. 18:5789-5802(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    3. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients."
      Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hematopoietic stem cell.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    7. "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.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLSM3_HUMAN
    AccessioniPrimary (citable) accession number: P62310
    Secondary accession number(s): Q6IAH0, Q9Y4Z1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 106 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3