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P97440

- SLBP_MOUSE

UniProt

P97440 - SLBP_MOUSE

Protein

Histone RNA hairpin-binding protein

Gene

Slbp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    RNA-binding protein involved in the histone pre-mRNA processing. Binds the stem-loop structure of replication-dependent histone pre-mRNAs and contributes to efficient 3'-end processing by stabilizing the complex between histone pre-mRNA and U7 small nuclear ribonucleoprotein (snRNP), via the histone downstream element (HDE). Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery. Stabilizes mature histone mRNA and could be involved in cell-cycle regulation of histone gene expression By similarity. Involved in the mechanism by which growing oocytes accumulate histone proteins that support early embryogenesis. Binds to the 5' side of the stem-loop structure of histone pre-mRNAs.By similarity2 Publications

    GO - Molecular functioni

    1. histone pre-mRNA stem-loop binding Source: UniProtKB
    2. mRNA binding Source: MGI

    GO - Biological processi

    1. histone mRNA 3'-end processing Source: UniProtKB
    2. mRNA transport Source: UniProtKB
    3. nuclear cell cycle DNA replication Source: UniProtKB

    Keywords - Molecular functioni

    Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone RNA hairpin-binding protein
    Alternative name(s):
    Histone stem-loop-binding protein
    Gene namesi
    Name:Slbp
    Synonyms:Hbp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:108402. Slbp.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Localizes predominantly in the nucleus at the G1/G2 phases and the beginning of S phase. Through the S phase, partially redistributes to the cytoplasm. Binding to histone mRNA is necessary for cytoplasmic localization. Shuttles between the nucleus and the cytoplasm. Imported in the nucleus by the Importin alpha/Importin beta receptor By similarity. Polyribosome-associated.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. histone pre-mRNA 3'end processing complex Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Females show no impaired oogenesis but display a defect in the formation of primordial follicles leading to infertility. Most embryos arrested at the 2-cell stage and fail to complete the second round of DNA replication due to an insufficient supply of histone H3 and H4. Accumulation of histone H2A and H2B is not affected.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 275275Histone RNA hairpin-binding proteinPRO_0000100357Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201PhosphoserineBy similarity
    Modified residuei23 – 231PhosphoserineBy similarity
    Modified residuei61 – 611Phosphothreonine; by CK2By similarity
    Modified residuei62 – 621Phosphothreonine; by CDK1By similarity
    Modified residuei171 – 1711PhosphothreonineBy similarity
    Modified residuei182 – 1821PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Thr-61 and Thr-62 in the S-phase. Phosphorylation of Thr-62 by CDK1 primes phosphorylation of Thr-61 by CK2. Phosphorylation of Thr-62 is required for its degradation at the end of the S phase. Its degradation is not required for histone mRNA degradation at the end of the S phase. All the phosphorylated forms detected are present in the cytoplasm. Both unphosphorylated and phosphorylated forms bind the stem-loop structure of histone mRNAs. Phosphorylation at Thr-171 increases affinity for histone mRNAs By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP97440.
    PRIDEiP97440.

    PTM databases

    PhosphoSiteiP97440.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in growing primary but not non-growing oocytes, within the primordial follicles. Also detected in fully-grown oocytes in antral follicles (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP97440.
    BgeeiP97440.
    CleanExiMM_SLBP.
    GenevestigatoriP97440.

    Interactioni

    Subunit structurei

    Monomer. SLBP/pre-mRNA complex interacts with ZNF473. Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1. Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase. Found in a ternary complex with ERI1 and the stem-loop structure of the 3' end of histone mRNA. Associates with polyribosomes By similarity. Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs.By similarity1 Publication

    Protein-protein interaction databases

    IntActiP97440. 1 interaction.
    MINTiMINT-8372793.

    Structurei

    3D structure databases

    ProteinModelPortaliP97440.
    SMRiP97440. Positions 127-199.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni129 – 19870RNA-bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi31 – 344Nuclear localization signal NLS1By similarity
    Motifi96 – 994Nuclear localization signal NLS2By similarity

    Domaini

    Amino acids 31-34, 96-99 and 246-249 are necessary for interaction with the Importin alpha/Importin beta receptor. The first 18 amino acids, amino acids 69-76 and 179-182 are necessary for interaction with TNPO3. Amino acids 31-34, 96-99 and 246-249 are necessary for nuclear localization By similarity.By similarity

    Sequence similaritiesi

    Belongs to the SLBP family.Curated

    Phylogenomic databases

    eggNOGiNOG278381.
    HOGENOMiHOG000065710.
    HOVERGENiHBG017805.
    InParanoidiP97440.
    OMAiKEVPRCH.
    PhylomeDBiP97440.
    TreeFamiTF316521.

    Family and domain databases

    InterProiIPR026502. SLBP1/SLBP2.
    IPR029344. SLBP_RNA_bind.
    [Graphical view]
    PANTHERiPTHR17408. PTHR17408. 1 hit.
    PfamiPF15247. SLBP_RNA_bind. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P97440-1 [UniParc]FASTAAdd to Basket

    « Hide

    MACRPRSPPG YGSRRDGGAS PRSPARWSLG RKRRADGRDR KPEDSEEGEL    50
    QTADHRPESF TTPEGHKPRS RCSDWASAVE EDEMRTRVNK EIARYKRKLL 100
    INDFGRERKS SSGSSDSKES MSSVPADVET DESVLMRRQK QINYGKNTIA 150
    YDRYIKEVPR HLRQPGIHPR TPNKFKKYSR RSWDQQIKLW KVALHFWDPP 200
    AEEGCDLQEI QPVDLGEMET EFTESSSESQ TSSQDNFDVY AGTPTKVRHV 250
    DCQVEDEFDL EACLTEPLKD FSAMS 275
    Length:275
    Mass (Da):31,603
    Last modified:May 1, 1997 - v1
    Checksum:i538459F001C59AF4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75680 mRNA. Translation: AAC53530.1.
    CCDSiCCDS19205.1.
    RefSeqiNP_033219.1. NM_009193.2.
    UniGeneiMm.4172.

    Genome annotation databases

    EnsembliENSMUST00000057551; ENSMUSP00000062930; ENSMUSG00000004642.
    GeneIDi20492.
    KEGGimmu:20492.
    UCSCiuc008xaw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U75680 mRNA. Translation: AAC53530.1 .
    CCDSi CCDS19205.1.
    RefSeqi NP_033219.1. NM_009193.2.
    UniGenei Mm.4172.

    3D structure databases

    ProteinModelPortali P97440.
    SMRi P97440. Positions 127-199.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P97440. 1 interaction.
    MINTi MINT-8372793.

    PTM databases

    PhosphoSitei P97440.

    Proteomic databases

    PaxDbi P97440.
    PRIDEi P97440.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000057551 ; ENSMUSP00000062930 ; ENSMUSG00000004642 .
    GeneIDi 20492.
    KEGGi mmu:20492.
    UCSCi uc008xaw.1. mouse.

    Organism-specific databases

    CTDi 7884.
    MGIi MGI:108402. Slbp.

    Phylogenomic databases

    eggNOGi NOG278381.
    HOGENOMi HOG000065710.
    HOVERGENi HBG017805.
    InParanoidi P97440.
    OMAi KEVPRCH.
    PhylomeDBi P97440.
    TreeFami TF316521.

    Miscellaneous databases

    NextBioi 298633.
    PROi P97440.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97440.
    Bgeei P97440.
    CleanExi MM_SLBP.
    Genevestigatori P97440.

    Family and domain databases

    InterProi IPR026502. SLBP1/SLBP2.
    IPR029344. SLBP_RNA_bind.
    [Graphical view ]
    PANTHERi PTHR17408. PTHR17408. 1 hit.
    Pfami PF15247. SLBP_RNA_bind. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing."
      Wang Z.-F., Whitfield M.L., Ingledue T.C. III, Dominski Z., Marzluff W.F.
      Genes Dev. 10:3028-3040(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NIH Swiss.
      Tissue: Embryo.
    2. "Stem-loop binding protein expressed in growing oocytes is required for accumulation of mRNAs encoding histones H3 and H4 and for early embryonic development in the mouse."
      Arnold D.R., Francon P., Zhang J., Martin K., Clarke H.J.
      Dev. Biol. 313:347-358(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Three proteins of the U7-specific Sm ring function as the molecular ruler to determine the site of 3'-end processing in mammalian histone pre-mRNA."
      Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.
      Mol. Cell. Biol. 29:4045-4056(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, RNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiSLBP_MOUSE
    AccessioniPrimary (citable) accession number: P97440
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3