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P97440 (SLBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone RNA hairpin-binding protein
Alternative name(s):
Histone stem-loop-binding protein
Gene names
Name:Slbp
Synonyms:Hbp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

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. Ref.2

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). Ref.2

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.

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.

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. Ref.2

Sequence similarities

Belongs to the SLBP family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 275275Histone RNA hairpin-binding protein
PRO_0000100357

Regions

Region129 – 19870RNA-binding By similarity
Motif31 – 344Nuclear localization signal NLS1 By similarity
Motif96 – 994Nuclear localization signal NLS2 By similarity

Amino acid modifications

Modified residue201Phosphoserine By similarity
Modified residue231Phosphoserine By similarity
Modified residue611Phosphothreonine; by CK2 By similarity
Modified residue621Phosphothreonine; by CDK1 By similarity
Modified residue1711Phosphothreonine By similarity
Modified residue1821Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P97440 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 538459F001C59AF4

FASTA27531,603
        10         20         30         40         50         60 
MACRPRSPPG YGSRRDGGAS PRSPARWSLG RKRRADGRDR KPEDSEEGEL QTADHRPESF 

        70         80         90        100        110        120 
TTPEGHKPRS RCSDWASAVE EDEMRTRVNK EIARYKRKLL INDFGRERKS SSGSSDSKES 

       130        140        150        160        170        180 
MSSVPADVET DESVLMRRQK QINYGKNTIA YDRYIKEVPR HLRQPGIHPR TPNKFKKYSR 

       190        200        210        220        230        240 
RSWDQQIKLW KVALHFWDPP AEEGCDLQEI QPVDLGEMET EFTESSSESQ TSSQDNFDVY 

       250        260        270 
AGTPTKVRHV DCQVEDEFDL EACLTEPLKD FSAMS 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U75680 mRNA. Translation: AAC53530.1.
CCDSCCDS19205.1.
RefSeqNP_033219.1. NM_009193.2.
UniGeneMm.4172.

3D structure databases

ProteinModelPortalP97440.
SMRP97440. Positions 127-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97440. 1 interaction.
MINTMINT-8372793.

PTM databases

PhosphoSiteP97440.

Proteomic databases

PaxDbP97440.
PRIDEP97440.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000057551; ENSMUSP00000062930; ENSMUSG00000004642.
GeneID20492.
KEGGmmu:20492.
UCSCuc008xaw.1. mouse.

Organism-specific databases

CTD7884.
MGIMGI:108402. Slbp.

Phylogenomic databases

eggNOGNOG278381.
HOGENOMHOG000065710.
HOVERGENHBG017805.
InParanoidP97440.
OMAKEVPRCH.
PhylomeDBP97440.
TreeFamTF316521.

Gene expression databases

ArrayExpressP97440.
BgeeP97440.
CleanExMM_SLBP.
GenevestigatorP97440.

Family and domain databases

InterProIPR026502. SLBP1/SLBP2.
IPR029344. SLBP_RNA_bind.
[Graphical view]
PANTHERPTHR17408. PTHR17408. 1 hit.
PfamPF15247. SLBP_RNA_bind. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio298633.
PROP97440.
SOURCESearch...

Entry information

Entry nameSLBP_MOUSE
AccessionPrimary (citable) accession number: P97440
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot