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Q9Y4Z0

- LSM4_HUMAN

UniProt

Q9Y4Z0 - LSM4_HUMAN

Protein

U6 snRNA-associated Sm-like protein LSm4

Gene

LSM4

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: UniProtKB

    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-KW
    5. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    6. RNA metabolic process Source: Reactome
    7. RNA splicing Source: ProtInc

    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 LSm4
    Alternative name(s):
    Glycine-rich protein
    Short name:
    GRP
    Gene namesi
    Name:LSM4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:17259. LSM4.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. small nuclear ribonucleoprotein complex Source: ProtInc
    3. spliceosomal complex Source: UniProtKB-KW
    4. U6 snRNP Source: ProtInc

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134906569.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 139139U6 snRNA-associated Sm-like protein LSm4PRO_0000125564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y4Z0.
    PaxDbiQ9Y4Z0.
    PeptideAtlasiQ9Y4Z0.
    PRIDEiQ9Y4Z0.

    PTM databases

    PhosphoSiteiQ9Y4Z0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y4Z0.
    BgeeiQ9Y4Z0.
    CleanExiHS_LSM4.
    GenevestigatoriQ9Y4Z0.

    Organism-specific databases

    HPAiHPA040932.

    Interactioni

    Subunit structurei

    LSm subunits form a heteromer with a doughnut shape.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM7Q9UK456EBI-372521,EBI-348372
    LSM8O957774EBI-372521,EBI-347779

    Protein-protein interaction databases

    BioGridi117336. 46 interactions.
    DIPiDIP-31209N.
    IntActiQ9Y4Z0. 16 interactions.
    MINTiMINT-1469332.
    STRINGi9606.ENSP00000252816.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y4Z0.
    SMRiQ9Y4Z0. Positions 14-71.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the snRNP Sm proteins family.Curated

    Phylogenomic databases

    eggNOGiCOG1958.
    HOGENOMiHOG000182713.
    HOVERGENiHBG000486.
    InParanoidiQ9Y4Z0.
    KOiK12623.
    OMAiWMNIHLV.
    OrthoDBiEOG747PMG.
    PhylomeDBiQ9Y4Z0.
    TreeFamiTF315027.

    Family and domain databases

    InterProiIPR027141. LSm4/Sm_D1/D3.
    IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view]
    PANTHERiPTHR23338. PTHR23338. 1 hit.
    PfamiPF01423. LSM. 1 hit.
    [Graphical view]
    SMARTiSM00651. Sm. 1 hit.
    [Graphical view]
    SUPFAMiSSF50182. SSF50182. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9Y4Z0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPLSLLKTA QNHPMLVELK NGETYNGHLV SCDNWMNINL REVICTSRDG    50
    DKFWRMPECY IRGSTIKYLR IPDEIIDMVK EEVVAKGRGR GGLQQQKQQK 100
    GRGMGGAGRG VFGGRGRGGI PGTGRGQPEK KPGRQAGKQ 139
    Length:139
    Mass (Da):15,350
    Last modified:November 1, 1999 - v1
    Checksum:iBCEFB20247335A1B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238096 mRNA. Translation: CAB45867.1.
    AF182290 mRNA. Translation: AAD56228.1.
    AF117235 mRNA. Translation: AAF17216.1.
    AF251218 mRNA. Translation: AAF90055.1.
    BC000387 mRNA. Translation: AAH00387.1.
    BC003652 mRNA. Translation: AAH03652.1.
    BC022198 mRNA. Translation: AAH22198.1.
    BC023665 mRNA. Translation: AAH23665.1.
    CCDSiCCDS12374.1.
    RefSeqiNP_036453.1. NM_012321.4.
    UniGeneiHs.515255.

    Genome annotation databases

    EnsembliENST00000593829; ENSP00000469468; ENSG00000130520.
    GeneIDi25804.
    KEGGihsa:25804.
    UCSCiuc002niq.3. human.

    Polymorphism databases

    DMDMi10720082.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ238096 mRNA. Translation: CAB45867.1 .
    AF182290 mRNA. Translation: AAD56228.1 .
    AF117235 mRNA. Translation: AAF17216.1 .
    AF251218 mRNA. Translation: AAF90055.1 .
    BC000387 mRNA. Translation: AAH00387.1 .
    BC003652 mRNA. Translation: AAH03652.1 .
    BC022198 mRNA. Translation: AAH22198.1 .
    BC023665 mRNA. Translation: AAH23665.1 .
    CCDSi CCDS12374.1.
    RefSeqi NP_036453.1. NM_012321.4.
    UniGenei Hs.515255.

    3D structure databases

    ProteinModelPortali Q9Y4Z0.
    SMRi Q9Y4Z0. Positions 14-71.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117336. 46 interactions.
    DIPi DIP-31209N.
    IntActi Q9Y4Z0. 16 interactions.
    MINTi MINT-1469332.
    STRINGi 9606.ENSP00000252816.

    PTM databases

    PhosphoSitei Q9Y4Z0.

    Polymorphism databases

    DMDMi 10720082.

    Proteomic databases

    MaxQBi Q9Y4Z0.
    PaxDbi Q9Y4Z0.
    PeptideAtlasi Q9Y4Z0.
    PRIDEi Q9Y4Z0.

    Protocols and materials databases

    DNASUi 25804.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000593829 ; ENSP00000469468 ; ENSG00000130520 .
    GeneIDi 25804.
    KEGGi hsa:25804.
    UCSCi uc002niq.3. human.

    Organism-specific databases

    CTDi 25804.
    GeneCardsi GC19M018417.
    HGNCi HGNC:17259. LSM4.
    HPAi HPA040932.
    MIMi 607284. gene.
    neXtProti NX_Q9Y4Z0.
    PharmGKBi PA134906569.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1958.
    HOGENOMi HOG000182713.
    HOVERGENi HBG000486.
    InParanoidi Q9Y4Z0.
    KOi K12623.
    OMAi WMNIHLV.
    OrthoDBi EOG747PMG.
    PhylomeDBi Q9Y4Z0.
    TreeFami TF315027.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi LSM4. human.
    GeneWikii LSM4.
    GenomeRNAii 25804.
    NextBioi 47015.
    PROi Q9Y4Z0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y4Z0.
    Bgeei Q9Y4Z0.
    CleanExi HS_LSM4.
    Genevestigatori Q9Y4Z0.

    Family and domain databases

    InterProi IPR027141. LSm4/Sm_D1/D3.
    IPR010920. LSM_dom.
    IPR001163. Ribonucl_LSM.
    IPR006649. Ribonucl_LSM_euk/arc.
    [Graphical view ]
    PANTHERi PTHR23338. PTHR23338. 1 hit.
    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: Liver.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hypothalamus.
    4. Chan E.K.L.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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: Lung.
    6. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-20, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLSM4_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y4Z0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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 19
      Human chromosome 19: 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