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)

O95777

- LSM8_HUMAN

UniProt

O95777 - LSM8_HUMAN

Protein

U6 snRNA-associated Sm-like protein LSm8

Gene

LSM8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Binds specifically to the 3'-terminal U-tract of U6 snRNA and is probably a component of the spliceosome.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. U6 snRNA binding Source: UniProtKB

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. RNA splicing Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    U6 snRNA-associated Sm-like protein LSm8
    Gene namesi
    Name:LSM8
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:20471. LSM8.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165618166.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 9695U6 snRNA-associated Sm-like protein LSm8PRO_0000125582Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO95777.
    PaxDbiO95777.
    PeptideAtlasiO95777.
    PRIDEiO95777.

    PTM databases

    PhosphoSiteiO95777.

    Expressioni

    Gene expression databases

    ArrayExpressiO95777.
    BgeeiO95777.
    CleanExiHS_LSM8.
    GenevestigatoriO95777.

    Organism-specific databases

    HPAiHPA020116.

    Interactioni

    Subunit structurei

    LSm subunits form a heteromer with a doughnut shape.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LSM2Q9Y3336EBI-347779,EBI-347416
    LSM3P623106EBI-347779,EBI-348239
    LSM4Q9Y4Z04EBI-347779,EBI-372521

    Protein-protein interaction databases

    BioGridi119679. 62 interactions.
    DIPiDIP-31195N.
    IntActiO95777. 51 interactions.
    MINTiMINT-1032595.
    STRINGi9606.ENSP00000249299.

    Structurei

    3D structure databases

    ProteinModelPortaliO95777.
    SMRiO95777. Positions 2-74.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the snRNP Sm proteins family.Curated

    Phylogenomic databases

    eggNOGiNOG235625.
    HOVERGENiHBG105578.
    InParanoidiO95777.
    KOiK12627.
    OMAiECHERVF.
    OrthoDBiEOG7SV0XS.
    PhylomeDBiO95777.
    TreeFamiTF314555.

    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.

    O95777-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSALENYIN RTVAVITSDG RMIVGTLKGF DQTINLILDE SHERVFSSSQ   50
    GVEQVVLGLY IVRGDNVAVI GEIDEETDSA LDLGNIRAEP LNSVAH 96
    Length:96
    Mass (Da):10,403
    Last modified:January 23, 2007 - v3
    Checksum:i15D26E6B75AA2EE1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF182294 mRNA. Translation: AAD56232.1.
    AC006389 Genomic DNA. Translation: AAD15542.1.
    BC002742 mRNA. Translation: AAH02742.1.
    BC022440 mRNA. Translation: AAH22440.1.
    CCDSiCCDS5775.1.
    RefSeqiNP_057284.1. NM_016200.4.
    UniGeneiHs.655046.

    Genome annotation databases

    EnsembliENST00000249299; ENSP00000249299; ENSG00000128534.
    GeneIDi51691.
    KEGGihsa:51691.
    UCSCiuc003vjg.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF182294 mRNA. Translation: AAD56232.1 .
    AC006389 Genomic DNA. Translation: AAD15542.1 .
    BC002742 mRNA. Translation: AAH02742.1 .
    BC022440 mRNA. Translation: AAH22440.1 .
    CCDSi CCDS5775.1.
    RefSeqi NP_057284.1. NM_016200.4.
    UniGenei Hs.655046.

    3D structure databases

    ProteinModelPortali O95777.
    SMRi O95777. Positions 2-74.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119679. 62 interactions.
    DIPi DIP-31195N.
    IntActi O95777. 51 interactions.
    MINTi MINT-1032595.
    STRINGi 9606.ENSP00000249299.

    PTM databases

    PhosphoSitei O95777.

    Proteomic databases

    MaxQBi O95777.
    PaxDbi O95777.
    PeptideAtlasi O95777.
    PRIDEi O95777.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000249299 ; ENSP00000249299 ; ENSG00000128534 .
    GeneIDi 51691.
    KEGGi hsa:51691.
    UCSCi uc003vjg.3. human.

    Organism-specific databases

    CTDi 51691.
    GeneCardsi GC07P117824.
    HGNCi HGNC:20471. LSM8.
    HPAi HPA020116.
    MIMi 607288. gene.
    neXtProti NX_O95777.
    PharmGKBi PA165618166.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235625.
    HOVERGENi HBG105578.
    InParanoidi O95777.
    KOi K12627.
    OMAi ECHERVF.
    OrthoDBi EOG7SV0XS.
    PhylomeDBi O95777.
    TreeFami TF314555.

    Miscellaneous databases

    GeneWikii LSM8.
    GenomeRNAii 51691.
    NextBioi 55698.
    PROi O95777.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95777.
    Bgeei O95777.
    CleanExi HS_LSM8.
    Genevestigatori O95777.

    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. "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.
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Brain and Uterus.
    4. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11; 29-44 AND 88-96, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLSM8_HUMAN
    AccessioniPrimary (citable) accession number: O95777
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 133 of the entry and version 3 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 7
      Human chromosome 7: 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