P97440 · SLBP_MOUSE

  • Protein
    Histone RNA hairpin-binding protein
  • Gene
    Slbp
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

RNA-binding protein involved in the histone pre-mRNA processing (PubMed:18036581).
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) (PubMed:18036581).
Plays an important role in targeting mature histone mRNA from the nucleus to the cytoplasm and to the translation machinery (By similarity).
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 (PubMed:18036581).
Binds to the 5' side of the stem-loop structure of histone pre-mRNAs (PubMed:19470752).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentcytosol
Cellular Componenthistone mRNA stem-loop binding complex
Cellular Componenthistone pre-mRNA 3'end processing complex
Cellular Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentribonucleoprotein complex
Molecular Functionhistone pre-mRNA stem-loop binding
Molecular Functionidentical protein binding
Molecular FunctionmRNA binding
Biological Processcap-dependent translational initiation
Biological ProcessmRNA 3'-end processing by stem-loop binding and cleavage
Biological ProcessmRNA transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone RNA hairpin-binding protein
  • Alternative names
    • Histone stem-loop-binding protein

Gene names

    • Name
      Slbp
    • Synonyms
      Hbp

Organism names

  • Taxonomic identifier
  • Strain
    • NIH Swiss
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P97440

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Nucleus
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

Keywords

Phenotypes & Variants

Disruption phenotype

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.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 14 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00001003571-275Histone RNA hairpin-binding protein
Modified residue20Phosphoserine
Modified residue23Phosphoserine
Modified residue59Phosphoserine
Modified residue61Phosphothreonine; by CK2
Modified residue62Phosphothreonine; by CDK1
Cross-link98Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue171Phosphothreonine
Modified residue182Phosphoserine

Post-translational modification

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).
Ubiquitinated by the CRL2(FEM1A), CRL2(FEM1B) and CRL2(FEM1C) complexes, leading to its degradation.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

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).

Gene expression databases

Interaction

Subunit

Monomer. SLBP/pre-mRNA complex interacts with ZNF473 (By similarity).
Interacts with the Importin alpha/Importin beta receptor, LSM1, MIF4GD, TNPO3 and UPF1 (By similarity).
Interaction with LSM1 occurs when histone mRNA is being rapidly degraded during the S phase (By similarity).
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 (PubMed:19470752).
Binds in a cooperative manner with ERI1 to the mature 3'-end of histone mRNAs (PubMed:19470752).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region1-88Disordered
Compositional bias29-88Basic and acidic residues
Motif31-34Nuclear localization signal NLS1
Motif96-99Nuclear localization signal NLS2
Region103-133Disordered
Region129-198RNA-binding
Region219-240Disordered
Compositional bias220-240Polar residues

Domain

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).

Sequence similarities

Belongs to the SLBP family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    275
  • Mass (Da)
    31,603
  • Last updated
    1997-05-01 v1
  • Checksum
    538459F001C59AF4
MACRPRSPPGYGSRRDGGASPRSPARWSLGRKRRADGRDRKPEDSEEGELQTADHRPESFTTPEGHKPRSRCSDWASAVEEDEMRTRVNKEIARYKRKLLINDFGRERKSSSGSSDSKESMSSVPADVETDESVLMRRQKQINYGKNTIAYDRYIKEVPRHLRQPGIHPRTPNKFKKYSRRSWDQQIKLWKVALHFWDPPAEEGCDLQEIQPVDLGEMETEFTESSSESQTSSQDNFDVYAGTPTKVRHVDCQVEDEFDLEACLTEPLKDFSAMS

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A0J9YV40A0A0J9YV40_MOUSESlbp219
Q8K2W7Q8K2W7_MOUSESlbp255
D3Z1S0D3Z1S0_MOUSESlbp33
Q3V2L1Q3V2L1_MOUSESlbp250

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias29-88Basic and acidic residues
Compositional bias220-240Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U75680
EMBL· GenBank· DDBJ
AAC53530.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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