P97440 (SLBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified February 19, 2014. Version 98. History...
Names and origin
|Protein names||Recommended name:|
Histone RNA hairpin-binding protein
Histone stem-loop-binding protein
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||275 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
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. Ref.2 Ref.3
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. Ref.3
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. Ref.2
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). Ref.2
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.
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.
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. Ref.2
Belongs to the SLBP family.
|Biological process||mRNA processing|
|Technical term||Complete proteome|
|Gene Ontology (GO)|
|Biological_process||histone mRNA 3'-end processingmRNA transport|
Inferred from sequence or structural similarity. Source: UniProtKBnuclear cell cycle DNA replication
Inferred from sequence or structural similarity. Source: UniProtKB
Inferred from sequence or structural similarity. Source: UniProtKBhistone pre-mRNA 3'end processing complex
|Molecular_function||histone pre-mRNA stem-loop bindingmRNA binding|
|Complete GO annotation...|
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 275||275||Histone RNA hairpin-binding protein||PRO_0000100357|
|Region||129 – 198||70||RNA-binding By similarity|
|Motif||31 – 34||4||Nuclear localization signal NLS1 By similarity|
|Motif||96 – 99||4||Nuclear localization signal NLS2 By similarity|
Amino acid modifications
|Modified residue||20||1||Phosphoserine By similarity|
|Modified residue||23||1||Phosphoserine By similarity|
|Modified residue||61||1||Phosphothreonine; by CK2 By similarity|
|Modified residue||62||1||Phosphothreonine; by CDK1 By similarity|
|Modified residue||171||1||Phosphothreonine By similarity|
|Modified residue||182||1||Phosphoserine By similarity|
|||"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.
|||"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.
|||"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.
|+||Additional computationally mapped references.|
|U75680 mRNA. Translation: AAC53530.1.|
|RefSeq||NP_033219.1. NM_009193.1. |
3D structure databases
|SMR||P97440. Positions 127-199. |
Protein-protein interaction databases
|IntAct||P97440. 1 interaction.|
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000057551; ENSMUSP00000062930; ENSMUSG00000004642. |
|UCSC||uc008xaw.1. mouse. |
|MGI||MGI:108402. Slbp. |
Gene expression databases
Family and domain databases
|InterPro||IPR026502. SLBP1/SLBP2. |
|PANTHER||PTHR17408. PTHR17408. 1 hit. |
|Accession||Primary (citable) accession number: P97440|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|